---
_id: '14281'
abstract:
- lang: eng
text: In nature, proteins that switch between two conformations in response to environmental
stimuli structurally transduce biochemical information in a manner analogous to
how transistors control information flow in computing devices. Designing proteins
with two distinct but fully structured conformations is a challenge for protein
design as it requires sculpting an energy landscape with two distinct minima.
Here we describe the design of “hinge” proteins that populate one designed state
in the absence of ligand and a second designed state in the presence of ligand.
X-ray crystallography, electron microscopy, double electron-electron resonance
spectroscopy, and binding measurements demonstrate that despite the significant
structural differences the two states are designed with atomic level accuracy
and that the conformational and binding equilibria are closely coupled.
article_processing_charge: No
article_type: original
author:
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Philip J. Y.
full_name: Leung, Philip J. Y.
last_name: Leung
- first_name: Maxx H.
full_name: Tessmer, Maxx H.
last_name: Tessmer
- first_name: Adam
full_name: Broerman, Adam
last_name: Broerman
- first_name: Cullen
full_name: Demakis, Cullen
last_name: Demakis
- first_name: Acacia F.
full_name: Dishman, Acacia F.
last_name: Dishman
- first_name: Arvind
full_name: Pillai, Arvind
last_name: Pillai
- first_name: Abbas
full_name: Idris, Abbas
last_name: Idris
- first_name: David
full_name: Juergens, David
last_name: Juergens
- first_name: Justas
full_name: Dauparas, Justas
last_name: Dauparas
- first_name: Xinting
full_name: Li, Xinting
last_name: Li
- first_name: Paul M.
full_name: Levine, Paul M.
last_name: Levine
- first_name: Mila
full_name: Lamb, Mila
last_name: Lamb
- first_name: Ryanne K.
full_name: Ballard, Ryanne K.
last_name: Ballard
- first_name: Stacey R.
full_name: Gerben, Stacey R.
last_name: Gerben
- first_name: Hannah
full_name: Nguyen, Hannah
last_name: Nguyen
- first_name: Alex
full_name: Kang, Alex
last_name: Kang
- first_name: Banumathi
full_name: Sankaran, Banumathi
last_name: Sankaran
- first_name: Asim K.
full_name: Bera, Asim K.
last_name: Bera
- first_name: Brian F.
full_name: Volkman, Brian F.
last_name: Volkman
- first_name: Jeff
full_name: Nivala, Jeff
last_name: Nivala
- first_name: Stefan
full_name: Stoll, Stefan
last_name: Stoll
- first_name: David
full_name: Baker, David
last_name: Baker
citation:
ama: Praetorius FM, Leung PJY, Tessmer MH, et al. Design of stimulus-responsive
two-state hinge proteins. Science. 2023;381(6659):754-760. doi:10.1126/science.adg7731
apa: Praetorius, F. M., Leung, P. J. Y., Tessmer, M. H., Broerman, A., Demakis,
C., Dishman, A. F., … Baker, D. (2023). Design of stimulus-responsive two-state
hinge proteins. Science. American Association for the Advancement of Science.
https://doi.org/10.1126/science.adg7731
chicago: Praetorius, Florian M, Philip J. Y. Leung, Maxx H. Tessmer, Adam Broerman,
Cullen Demakis, Acacia F. Dishman, Arvind Pillai, et al. “Design of Stimulus-Responsive
Two-State Hinge Proteins.” Science. American Association for the Advancement
of Science, 2023. https://doi.org/10.1126/science.adg7731.
ieee: F. M. Praetorius et al., “Design of stimulus-responsive two-state hinge
proteins,” Science, vol. 381, no. 6659. American Association for the Advancement
of Science, pp. 754–760, 2023.
ista: Praetorius FM, Leung PJY, Tessmer MH, Broerman A, Demakis C, Dishman AF, Pillai
A, Idris A, Juergens D, Dauparas J, Li X, Levine PM, Lamb M, Ballard RK, Gerben
SR, Nguyen H, Kang A, Sankaran B, Bera AK, Volkman BF, Nivala J, Stoll S, Baker
D. 2023. Design of stimulus-responsive two-state hinge proteins. Science. 381(6659),
754–760.
mla: Praetorius, Florian M., et al. “Design of Stimulus-Responsive Two-State Hinge
Proteins.” Science, vol. 381, no. 6659, American Association for the Advancement
of Science, 2023, pp. 754–60, doi:10.1126/science.adg7731.
short: F.M. Praetorius, P.J.Y. Leung, M.H. Tessmer, A. Broerman, C. Demakis, A.F.
Dishman, A. Pillai, A. Idris, D. Juergens, J. Dauparas, X. Li, P.M. Levine, M.
Lamb, R.K. Ballard, S.R. Gerben, H. Nguyen, A. Kang, B. Sankaran, A.K. Bera, B.F.
Volkman, J. Nivala, S. Stoll, D. Baker, Science 381 (2023) 754–760.
date_created: 2023-09-06T12:04:23Z
date_published: 2023-08-17T00:00:00Z
date_updated: 2023-11-07T12:42:09Z
day: '17'
doi: 10.1126/science.adg7731
extern: '1'
external_id:
pmid:
- '37590357'
intvolume: ' 381'
issue: '6659'
language:
- iso: eng
month: '08'
oa_version: None
page: 754-760
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Design of stimulus-responsive two-state hinge proteins
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 381
year: '2023'
...
---
_id: '14294'
abstract:
- lang: eng
text: Growth factors and cytokines signal by binding to the extracellular domains
of their receptors and drive association and transphosphorylation of the receptor
intracellular tyrosine kinase domains, initiating downstream signaling cascades.
To enable systematic exploration of how receptor valency and geometry affects
signaling outcomes, we designed cyclic homo-oligomers with up to 8 subunits using
repeat protein building blocks that can be modularly extended. By incorporating
a de novo designed fibroblast growth-factor receptor (FGFR) binding module into
these scaffolds, we generated a series of synthetic signaling ligands that exhibit
potent valency- and geometry-dependent Ca2+ release and MAPK pathway activation.
The high specificity of the designed agonists reveal distinct roles for two FGFR
splice variants in driving endothelial and mesenchymal cell fates during early
vascular development. The ability to incorporate receptor binding domains and
repeat extensions in a modular fashion makes our designed scaffolds broadly useful
for probing and manipulating cellular signaling pathways.
article_processing_charge: No
author:
- first_name: Natasha I
full_name: Edman, Natasha I
last_name: Edman
- first_name: Rachel L
full_name: Redler, Rachel L
last_name: Redler
- first_name: Ashish
full_name: Phal, Ashish
last_name: Phal
- first_name: Thomas
full_name: Schlichthaerle, Thomas
last_name: Schlichthaerle
- first_name: Sanjay R
full_name: Srivatsan, Sanjay R
last_name: Srivatsan
- first_name: Ali
full_name: Etemadi, Ali
last_name: Etemadi
- first_name: Seong
full_name: An, Seong
last_name: An
- first_name: Andrew
full_name: Favor, Andrew
last_name: Favor
- first_name: Devon
full_name: Ehnes, Devon
last_name: Ehnes
- first_name: Zhe
full_name: Li, Zhe
last_name: Li
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Max
full_name: Gordon, Max
last_name: Gordon
- first_name: Wei
full_name: Yang, Wei
last_name: Yang
- first_name: Brian
full_name: Coventry, Brian
last_name: Coventry
- first_name: Derrick R
full_name: Hicks, Derrick R
last_name: Hicks
- first_name: Longxing
full_name: Cao, Longxing
last_name: Cao
- first_name: Neville
full_name: Bethel, Neville
last_name: Bethel
- first_name: Piper
full_name: Heine, Piper
last_name: Heine
- first_name: Analisa N
full_name: Murray, Analisa N
last_name: Murray
- first_name: Stacey
full_name: Gerben, Stacey
last_name: Gerben
- first_name: Lauren
full_name: Carter, Lauren
last_name: Carter
- first_name: Marcos
full_name: Miranda, Marcos
last_name: Miranda
- first_name: Babak
full_name: Negahdari, Babak
last_name: Negahdari
- first_name: Sangwon
full_name: Lee, Sangwon
last_name: Lee
- first_name: Cole
full_name: Trapnell, Cole
last_name: Trapnell
- first_name: Lance
full_name: Stewart, Lance
last_name: Stewart
- first_name: Damian C
full_name: Ekiert, Damian C
last_name: Ekiert
- first_name: Joseph
full_name: Schlessinger, Joseph
last_name: Schlessinger
- first_name: Jay
full_name: Shendure, Jay
last_name: Shendure
- first_name: Gira
full_name: Bhabha, Gira
last_name: Bhabha
- first_name: Hannele
full_name: Ruohola-Baker, Hannele
last_name: Ruohola-Baker
- first_name: David
full_name: Baker, David
last_name: Baker
citation:
ama: Edman NI, Redler RL, Phal A, et al. Modulation of FGF pathway signaling and
vascular differentiation using designed oligomeric assemblies. bioRxiv.
doi:10.1101/2023.03.14.532666
apa: Edman, N. I., Redler, R. L., Phal, A., Schlichthaerle, T., Srivatsan, S. R.,
Etemadi, A., … Baker, D. (n.d.). Modulation of FGF pathway signaling and vascular
differentiation using designed oligomeric assemblies. bioRxiv. https://doi.org/10.1101/2023.03.14.532666
chicago: Edman, Natasha I, Rachel L Redler, Ashish Phal, Thomas Schlichthaerle,
Sanjay R Srivatsan, Ali Etemadi, Seong An, et al. “Modulation of FGF Pathway Signaling
and Vascular Differentiation Using Designed Oligomeric Assemblies.” BioRxiv,
n.d. https://doi.org/10.1101/2023.03.14.532666.
ieee: N. I. Edman et al., “Modulation of FGF pathway signaling and vascular
differentiation using designed oligomeric assemblies,” bioRxiv. .
ista: Edman NI, Redler RL, Phal A, Schlichthaerle T, Srivatsan SR, Etemadi A, An
S, Favor A, Ehnes D, Li Z, Praetorius FM, Gordon M, Yang W, Coventry B, Hicks
DR, Cao L, Bethel N, Heine P, Murray AN, Gerben S, Carter L, Miranda M, Negahdari
B, Lee S, Trapnell C, Stewart L, Ekiert DC, Schlessinger J, Shendure J, Bhabha
G, Ruohola-Baker H, Baker D. Modulation of FGF pathway signaling and vascular
differentiation using designed oligomeric assemblies. bioRxiv, 10.1101/2023.03.14.532666.
mla: Edman, Natasha I., et al. “Modulation of FGF Pathway Signaling and Vascular
Differentiation Using Designed Oligomeric Assemblies.” BioRxiv, doi:10.1101/2023.03.14.532666.
short: N.I. Edman, R.L. Redler, A. Phal, T. Schlichthaerle, S.R. Srivatsan, A. Etemadi,
S. An, A. Favor, D. Ehnes, Z. Li, F.M. Praetorius, M. Gordon, W. Yang, B. Coventry,
D.R. Hicks, L. Cao, N. Bethel, P. Heine, A.N. Murray, S. Gerben, L. Carter, M.
Miranda, B. Negahdari, S. Lee, C. Trapnell, L. Stewart, D.C. Ekiert, J. Schlessinger,
J. Shendure, G. Bhabha, H. Ruohola-Baker, D. Baker, BioRxiv (n.d.).
date_created: 2023-09-06T12:31:49Z
date_published: 2023-03-15T00:00:00Z
date_updated: 2023-11-07T12:21:58Z
day: '15'
doi: 10.1101/2023.03.14.532666
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2023.03.14.532666
month: '03'
oa: 1
oa_version: Preprint
publication: bioRxiv
publication_status: submitted
status: public
title: Modulation of FGF pathway signaling and vascular differentiation using designed
oligomeric assemblies
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '14282'
abstract:
- lang: eng
text: Asymmetric multiprotein complexes that undergo subunit exchange play central
roles in biology but present a challenge for design because the components must
not only contain interfaces that enable reversible association but also be stable
and well behaved in isolation. We use implicit negative design to generate β sheet–mediated
heterodimers that can be assembled into a wide variety of complexes. The designs
are stable, folded, and soluble in isolation and rapidly assemble upon mixing,
and crystal structures are close to the computational models. We construct linearly
arranged hetero-oligomers with up to six different components, branched hetero-oligomers,
closed C4-symmetric two-component rings, and hetero-oligomers assembled on a cyclic
homo-oligomeric central hub and demonstrate that such complexes can readily reconfigure
through subunit exchange. Our approach provides a general route to designing asymmetric
reconfigurable protein systems.
article_number: abj7662
article_processing_charge: No
article_type: original
author:
- first_name: Danny D.
full_name: Sahtoe, Danny D.
last_name: Sahtoe
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Alexis
full_name: Courbet, Alexis
last_name: Courbet
- first_name: Yang
full_name: Hsia, Yang
last_name: Hsia
- first_name: Basile I. M.
full_name: Wicky, Basile I. M.
last_name: Wicky
- first_name: Natasha I.
full_name: Edman, Natasha I.
last_name: Edman
- first_name: Lauren M.
full_name: Miller, Lauren M.
last_name: Miller
- first_name: Bart J. R.
full_name: Timmermans, Bart J. R.
last_name: Timmermans
- first_name: Justin
full_name: Decarreau, Justin
last_name: Decarreau
- first_name: Hana M.
full_name: Morris, Hana M.
last_name: Morris
- first_name: Alex
full_name: Kang, Alex
last_name: Kang
- first_name: Asim K.
full_name: Bera, Asim K.
last_name: Bera
- first_name: David
full_name: Baker, David
last_name: Baker
citation:
ama: Sahtoe DD, Praetorius FM, Courbet A, et al. Reconfigurable asymmetric protein
assemblies through implicit negative design. Science. 2022;375(6578). doi:10.1126/science.abj7662
apa: Sahtoe, D. D., Praetorius, F. M., Courbet, A., Hsia, Y., Wicky, B. I. M., Edman,
N. I., … Baker, D. (2022). Reconfigurable asymmetric protein assemblies through
implicit negative design. Science. American Association for the Advancement
of Science. https://doi.org/10.1126/science.abj7662
chicago: Sahtoe, Danny D., Florian M Praetorius, Alexis Courbet, Yang Hsia, Basile
I. M. Wicky, Natasha I. Edman, Lauren M. Miller, et al. “Reconfigurable Asymmetric
Protein Assemblies through Implicit Negative Design.” Science. American
Association for the Advancement of Science, 2022. https://doi.org/10.1126/science.abj7662.
ieee: D. D. Sahtoe et al., “Reconfigurable asymmetric protein assemblies
through implicit negative design,” Science, vol. 375, no. 6578. American
Association for the Advancement of Science, 2022.
ista: Sahtoe DD, Praetorius FM, Courbet A, Hsia Y, Wicky BIM, Edman NI, Miller LM,
Timmermans BJR, Decarreau J, Morris HM, Kang A, Bera AK, Baker D. 2022. Reconfigurable
asymmetric protein assemblies through implicit negative design. Science. 375(6578),
abj7662.
mla: Sahtoe, Danny D., et al. “Reconfigurable Asymmetric Protein Assemblies through
Implicit Negative Design.” Science, vol. 375, no. 6578, abj7662, American
Association for the Advancement of Science, 2022, doi:10.1126/science.abj7662.
short: D.D. Sahtoe, F.M. Praetorius, A. Courbet, Y. Hsia, B.I.M. Wicky, N.I. Edman,
L.M. Miller, B.J.R. Timmermans, J. Decarreau, H.M. Morris, A. Kang, A.K. Bera,
D. Baker, Science 375 (2022).
date_created: 2023-09-06T12:05:42Z
date_published: 2022-01-21T00:00:00Z
date_updated: 2023-11-07T12:39:56Z
day: '21'
doi: 10.1126/science.abj7662
extern: '1'
external_id:
pmid:
- '35050655'
intvolume: ' 375'
issue: '6578'
language:
- iso: eng
month: '01'
oa_version: None
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Reconfigurable asymmetric protein assemblies through implicit negative design
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 375
year: '2022'
...
---
_id: '14299'
abstract:
- lang: eng
text: DNA origami nano-objects are usually designed around generic single-stranded
“scaffolds”. Many properties of the target object are determined by details of
those generic scaffold sequences. Here, we enable designers to fully specify the
target structure not only in terms of desired 3D shape but also in terms of the
sequences used. To this end, we built design tools to construct scaffold sequences
de novo based on strand diagrams, and we developed scalable production methods
for creating design-specific scaffold strands with fully user-defined sequences.
We used 17 custom scaffolds having different lengths and sequence properties to
study the influence of sequence redundancy and sequence composition on multilayer
DNA origami assembly and to realize efficient one-pot assembly of multiscaffold
DNA origami objects. Furthermore, as examples for functionalized scaffolds, we
created a scaffold that enables direct, covalent cross-linking of DNA origami
via UV irradiation, and we built DNAzyme-containing scaffolds that allow postfolding
DNA origami domain separation.
article_processing_charge: No
article_type: original
author:
- first_name: Engelhardt
full_name: FAS, Engelhardt
last_name: FAS
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: CH
full_name: Wachauf, CH
last_name: Wachauf
- first_name: G
full_name: Brüggenthies, G
last_name: Brüggenthies
- first_name: F
full_name: Kohler, F
last_name: Kohler
- first_name: B
full_name: Kick, B
last_name: Kick
- first_name: KL
full_name: Kadletz, KL
last_name: Kadletz
- first_name: PN
full_name: Pham, PN
last_name: Pham
- first_name: KL
full_name: Behler, KL
last_name: Behler
- first_name: T
full_name: Gerling, T
last_name: Gerling
- first_name: H
full_name: Dietz, H
last_name: Dietz
citation:
ama: FAS E, Praetorius FM, Wachauf C, et al. Custom-size, functional, and durable
DNA origami with design-specific scaffolds. ACS Nano. 2019;13(5):5015-5027.
doi:10.1021/acsnano.9b01025
apa: FAS, E., Praetorius, F. M., Wachauf, C., Brüggenthies, G., Kohler, F., Kick,
B., … Dietz, H. (2019). Custom-size, functional, and durable DNA origami with
design-specific scaffolds. ACS Nano. ACS Publications. https://doi.org/10.1021/acsnano.9b01025
chicago: FAS, Engelhardt, Florian M Praetorius, CH Wachauf, G Brüggenthies, F Kohler,
B Kick, KL Kadletz, et al. “Custom-Size, Functional, and Durable DNA Origami with
Design-Specific Scaffolds.” ACS Nano. ACS Publications, 2019. https://doi.org/10.1021/acsnano.9b01025.
ieee: E. FAS et al., “Custom-size, functional, and durable DNA origami with
design-specific scaffolds,” ACS Nano, vol. 13, no. 5. ACS Publications,
pp. 5015–5027, 2019.
ista: FAS E, Praetorius FM, Wachauf C, Brüggenthies G, Kohler F, Kick B, Kadletz
K, Pham P, Behler K, Gerling T, Dietz H. 2019. Custom-size, functional, and durable
DNA origami with design-specific scaffolds. ACS Nano. 13(5), 5015–5027.
mla: FAS, Engelhardt, et al. “Custom-Size, Functional, and Durable DNA Origami with
Design-Specific Scaffolds.” ACS Nano, vol. 13, no. 5, ACS Publications,
2019, pp. 5015–27, doi:10.1021/acsnano.9b01025.
short: E. FAS, F.M. Praetorius, C. Wachauf, G. Brüggenthies, F. Kohler, B. Kick,
K. Kadletz, P. Pham, K. Behler, T. Gerling, H. Dietz, ACS Nano 13 (2019) 5015–5027.
date_created: 2023-09-06T12:48:47Z
date_published: 2019-04-16T00:00:00Z
date_updated: 2023-11-07T12:17:31Z
day: '16'
doi: 10.1021/acsnano.9b01025
extern: '1'
external_id:
pmid:
- '30990672'
intvolume: ' 13'
issue: '5'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1021/acsnano.9b01025
month: '04'
oa: 1
oa_version: Published Version
page: 5015-5027
pmid: 1
publication: ACS Nano
publication_identifier:
eissn:
- 1936-086x
issn:
- 1936-0851
publication_status: published
publisher: ACS Publications
quality_controlled: '1'
scopus_import: '1'
status: public
title: Custom-size, functional, and durable DNA origami with design-specific scaffolds
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 13
year: '2019'
...
---
_id: '14284'
abstract:
- lang: eng
text: Pore-forming toxins (PFT) are virulence factors that transform from soluble
to membrane-bound states. The Yersinia YaxAB system represents a family of binary
α-PFTs with orthologues in human, insect, and plant pathogens, with unknown structures.
YaxAB was shown to be cytotoxic and likely involved in pathogenesis, though the
molecular basis for its two-component lytic mechanism remains elusive. Here, we
present crystal structures of YaxA and YaxB, together with a cryo-electron microscopy
map of the YaxAB complex. Our structures reveal a pore predominantly composed
of decamers of YaxA–YaxB heterodimers. Both subunits bear membrane-active moieties,
but only YaxA is capable of binding to membranes by itself. YaxB can subsequently
be recruited to membrane-associated YaxA and induced to present its lytic transmembrane
helices. Pore formation can progress by further oligomerization of YaxA–YaxB dimers.
Our results allow for a comparison between pore assemblies belonging to the wider
ClyA-like family of α-PFTs, highlighting diverse pore architectures.
article_number: '1806'
article_processing_charge: No
article_type: original
author:
- first_name: Bastian
full_name: Bräuning, Bastian
last_name: Bräuning
- first_name: Eva
full_name: Bertosin, Eva
last_name: Bertosin
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Christian
full_name: Ihling, Christian
last_name: Ihling
- first_name: Alexandra
full_name: Schatt, Alexandra
last_name: Schatt
- first_name: Agnes
full_name: Adler, Agnes
last_name: Adler
- first_name: Klaus
full_name: Richter, Klaus
last_name: Richter
- first_name: Andrea
full_name: Sinz, Andrea
last_name: Sinz
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
- first_name: Michael
full_name: Groll, Michael
last_name: Groll
citation:
ama: Bräuning B, Bertosin E, Praetorius FM, et al. Structure and mechanism of the
two-component α-helical pore-forming toxin YaxAB. Nature Communications.
2018;9. doi:10.1038/s41467-018-04139-2
apa: Bräuning, B., Bertosin, E., Praetorius, F. M., Ihling, C., Schatt, A., Adler,
A., … Groll, M. (2018). Structure and mechanism of the two-component α-helical
pore-forming toxin YaxAB. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-018-04139-2
chicago: Bräuning, Bastian, Eva Bertosin, Florian M Praetorius, Christian Ihling,
Alexandra Schatt, Agnes Adler, Klaus Richter, Andrea Sinz, Hendrik Dietz, and
Michael Groll. “Structure and Mechanism of the Two-Component α-Helical Pore-Forming
Toxin YaxAB.” Nature Communications. Springer Nature, 2018. https://doi.org/10.1038/s41467-018-04139-2.
ieee: B. Bräuning et al., “Structure and mechanism of the two-component α-helical
pore-forming toxin YaxAB,” Nature Communications, vol. 9. Springer Nature,
2018.
ista: Bräuning B, Bertosin E, Praetorius FM, Ihling C, Schatt A, Adler A, Richter
K, Sinz A, Dietz H, Groll M. 2018. Structure and mechanism of the two-component
α-helical pore-forming toxin YaxAB. Nature Communications. 9, 1806.
mla: Bräuning, Bastian, et al. “Structure and Mechanism of the Two-Component α-Helical
Pore-Forming Toxin YaxAB.” Nature Communications, vol. 9, 1806, Springer
Nature, 2018, doi:10.1038/s41467-018-04139-2.
short: B. Bräuning, E. Bertosin, F.M. Praetorius, C. Ihling, A. Schatt, A. Adler,
K. Richter, A. Sinz, H. Dietz, M. Groll, Nature Communications 9 (2018).
date_created: 2023-09-06T12:07:33Z
date_published: 2018-05-04T00:00:00Z
date_updated: 2023-11-07T11:46:12Z
day: '04'
doi: 10.1038/s41467-018-04139-2
extern: '1'
external_id:
pmid:
- '29728606'
intvolume: ' 9'
keyword:
- General Physics and Astronomy
- General Biochemistry
- Genetics and Molecular Biology
- General Chemistry
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41467-018-04139-2
month: '05'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2018'
...
---
_id: '14306'
abstract:
- lang: eng
text: 'Function and activity of biomolecules often depend on their spatial arrangement.
The method introduced here allows genetically encoding the spatial arrangement
of proteins and DNA. The approach relies on staple proteins that fold double-stranded
DNA into user-defined shapes. This thesis describes the development of staple
proteins based on the DNA recognition of TAL effectors and presents experimentally
derived rules for designing a variety of self-assembling nanoscale shapes featuring
structural motifs such as curvature, vertices, corners, and multilayer helix packing. '
article_processing_charge: No
author:
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
citation:
ama: Praetorius FM. Genetically encoding the spatial arrangement of DNA and proteins
in self-assembling nanostructures. 2018.
apa: Praetorius, F. M. (2018). Genetically encoding the spatial arrangement of
DNA and proteins in self-assembling nanostructures. Technische Universität
München.
chicago: Praetorius, Florian M. “Genetically Encoding the Spatial Arrangement of
DNA and Proteins in Self-Assembling Nanostructures.” Technische Universität München,
2018.
ieee: F. M. Praetorius, “Genetically encoding the spatial arrangement of DNA and
proteins in self-assembling nanostructures,” Technische Universität München, 2018.
ista: Praetorius FM. 2018. Genetically encoding the spatial arrangement of DNA and
proteins in self-assembling nanostructures. Technische Universität München.
mla: Praetorius, Florian M. Genetically Encoding the Spatial Arrangement of DNA
and Proteins in Self-Assembling Nanostructures. Technische Universität München,
2018.
short: F.M. Praetorius, Genetically Encoding the Spatial Arrangement of DNA and
Proteins in Self-Assembling Nanostructures, Technische Universität München, 2018.
date_created: 2023-09-06T13:11:22Z
date_published: 2018-01-16T00:00:00Z
date_updated: 2023-11-07T11:43:38Z
day: '16'
degree_awarded: PhD
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://mediatum.ub.tum.de/1398662
month: '01'
oa: 1
oa_version: Published Version
publication_status: published
publisher: Technische Universität München
status: public
supervisor:
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
title: Genetically encoding the spatial arrangement of DNA and proteins in self-assembling
nanostructures
type: dissertation
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2018'
...
---
_id: '14310'
article_processing_charge: No
author:
- first_name: Mahsa
full_name: Siavashpouri, Mahsa
last_name: Siavashpouri
- first_name: Christian
full_name: Wachauf, Christian
last_name: Wachauf
- first_name: Mark
full_name: Zakhary, Mark
last_name: Zakhary
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
- first_name: Zvonimir
full_name: Dogic, Zvonimir
last_name: Dogic
citation:
ama: 'Siavashpouri M, Wachauf C, Zakhary M, Praetorius FM, Dietz H, Dogic Z. Molecular
engineering of colloidal liquid crystals using DNA origami. In: APS March Meeting
2017. APS; 2017.'
apa: Siavashpouri, M., Wachauf, C., Zakhary, M., Praetorius, F. M., Dietz, H., &
Dogic, Z. (2017). Molecular engineering of colloidal liquid crystals using DNA
origami. In APS March Meeting 2017. APS.
chicago: Siavashpouri, Mahsa, Christian Wachauf, Mark Zakhary, Florian M Praetorius,
Hendrik Dietz, and Zvonimir Dogic. “Molecular Engineering of Colloidal Liquid
Crystals Using DNA Origami.” In APS March Meeting 2017. APS, 2017.
ieee: M. Siavashpouri, C. Wachauf, M. Zakhary, F. M. Praetorius, H. Dietz, and Z.
Dogic, “Molecular engineering of colloidal liquid crystals using DNA origami,”
in APS March Meeting 2017, 2017.
ista: Siavashpouri M, Wachauf C, Zakhary M, Praetorius FM, Dietz H, Dogic Z. 2017.
Molecular engineering of colloidal liquid crystals using DNA origami. APS March
Meeting 2017. .
mla: Siavashpouri, Mahsa, et al. “Molecular Engineering of Colloidal Liquid Crystals
Using DNA Origami.” APS March Meeting 2017, APS, 2017.
short: M. Siavashpouri, C. Wachauf, M. Zakhary, F.M. Praetorius, H. Dietz, Z. Dogic,
in:, APS March Meeting 2017, APS, 2017.
date_created: 2023-09-06T13:40:20Z
date_published: 2017-03-01T00:00:00Z
date_updated: 2023-11-07T11:36:15Z
day: '01'
extern: '1'
language:
- iso: eng
month: '03'
oa_version: None
publication: APS March Meeting 2017
publication_status: published
publisher: APS
quality_controlled: '1'
status: public
title: Molecular engineering of colloidal liquid crystals using DNA origami
type: conference_abstract
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2017'
...
---
_id: '14286'
abstract:
- lang: eng
text: 'The bacteriophage M13 has found frequent applications in nanobiotechnology
due to its chemically and genetically tunable protein surface and its ability
to self-assemble into colloidal membranes. Additionally, its single-stranded (ss)
genome is commonly used as scaffold for DNA origami. Despite the manifold uses
of M13, upstream production methods for phage and scaffold ssDNA are underexamined
with respect to future industrial usage. Here, the high-cell-density phage production
with Escherichia coli as host organism was studied in respect of medium composition,
infection time, multiplicity of infection, and specific growth rate. The specific
growth rate and the multiplicity of infection were identified as the crucial state
variables that influence phage amplification rate on one hand and the concentration
of produced ssDNA on the other hand. Using a growth rate of 0.15 h−1 and a multiplicity
of infection of 0.05 pfu cfu−1 in the fed-batch production process, the concentration
of pure isolated M13 ssDNA usable for scaffolded DNA origami could be enhanced
by 54% to 590 mg L−1. Thus, our results help enabling M13 production for industrial
uses in nanobiotechnology. Biotechnol. Bioeng. 2017;114: 777–784.'
article_processing_charge: No
article_type: original
author:
- first_name: Benjamin
full_name: Kick, Benjamin
last_name: Kick
- first_name: Samantha
full_name: Hensler, Samantha
last_name: Hensler
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
- first_name: Dirk
full_name: Weuster-Botz, Dirk
last_name: Weuster-Botz
citation:
ama: Kick B, Hensler S, Praetorius FM, Dietz H, Weuster-Botz D. Specific growth
rate and multiplicity of infection affect high-cell-density fermentation with
bacteriophage M13 for ssDNA production. Biotechnology and Bioengineering.
2017;114(4):777-784. doi:10.1002/bit.26200
apa: Kick, B., Hensler, S., Praetorius, F. M., Dietz, H., & Weuster-Botz, D.
(2017). Specific growth rate and multiplicity of infection affect high-cell-density
fermentation with bacteriophage M13 for ssDNA production. Biotechnology and
Bioengineering. Wiley. https://doi.org/10.1002/bit.26200
chicago: Kick, Benjamin, Samantha Hensler, Florian M Praetorius, Hendrik Dietz,
and Dirk Weuster-Botz. “Specific Growth Rate and Multiplicity of Infection Affect
High-Cell-Density Fermentation with Bacteriophage M13 for SsDNA Production.” Biotechnology
and Bioengineering. Wiley, 2017. https://doi.org/10.1002/bit.26200.
ieee: B. Kick, S. Hensler, F. M. Praetorius, H. Dietz, and D. Weuster-Botz, “Specific
growth rate and multiplicity of infection affect high-cell-density fermentation
with bacteriophage M13 for ssDNA production,” Biotechnology and Bioengineering,
vol. 114, no. 4. Wiley, pp. 777–784, 2017.
ista: Kick B, Hensler S, Praetorius FM, Dietz H, Weuster-Botz D. 2017. Specific
growth rate and multiplicity of infection affect high-cell-density fermentation
with bacteriophage M13 for ssDNA production. Biotechnology and Bioengineering.
114(4), 777–784.
mla: Kick, Benjamin, et al. “Specific Growth Rate and Multiplicity of Infection
Affect High-Cell-Density Fermentation with Bacteriophage M13 for SsDNA Production.”
Biotechnology and Bioengineering, vol. 114, no. 4, Wiley, 2017, pp. 777–84,
doi:10.1002/bit.26200.
short: B. Kick, S. Hensler, F.M. Praetorius, H. Dietz, D. Weuster-Botz, Biotechnology
and Bioengineering 114 (2017) 777–784.
date_created: 2023-09-06T12:08:29Z
date_published: 2017-04-01T00:00:00Z
date_updated: 2023-11-07T12:36:20Z
day: '01'
doi: 10.1002/bit.26200
extern: '1'
external_id:
pmid:
- '27748519'
intvolume: ' 114'
issue: '4'
keyword:
- Applied Microbiology and Biotechnology
- Bioengineering
- Biotechnology
language:
- iso: eng
month: '04'
oa_version: None
page: 777-784
pmid: 1
publication: Biotechnology and Bioengineering
publication_identifier:
issn:
- 0006-3592
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: Specific growth rate and multiplicity of infection affect high-cell-density
fermentation with bacteriophage M13 for ssDNA production
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 114
year: '2017'
...
---
_id: '14287'
abstract:
- lang: eng
text: We describe an approach to bottom-up fabrication that allows integration of
the functional diversity of proteins into designed three-dimensional structural
frameworks. A set of custom staple proteins based on transcription activator–like
effector proteins folds a double-stranded DNA template into a user-defined shape.
Each staple protein is designed to recognize and closely link two distinct double-helical
DNA sequences at separate positions on the template. We present design rules for
constructing megadalton-scale DNA-protein hybrid shapes; introduce various structural
motifs, such as custom curvature, corners, and vertices; and describe principles
for creating multilayer DNA-protein objects with enhanced rigidity. We demonstrate
self-assembly of our hybrid nanostructures in one-pot mixtures that include the
genetic information for the designed proteins, the template DNA, RNA polymerase,
ribosomes, and cofactors for transcription and translation.
article_number: eaam5488
article_processing_charge: No
article_type: original
author:
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
citation:
ama: Praetorius FM, Dietz H. Self-assembly of genetically encoded DNA-protein hybrid
nanoscale shapes. Science. 2017;355(6331). doi:10.1126/science.aam5488
apa: Praetorius, F. M., & Dietz, H. (2017). Self-assembly of genetically encoded
DNA-protein hybrid nanoscale shapes. Science. American Association for
the Advancement of Science. https://doi.org/10.1126/science.aam5488
chicago: Praetorius, Florian M, and Hendrik Dietz. “Self-Assembly of Genetically
Encoded DNA-Protein Hybrid Nanoscale Shapes.” Science. American Association
for the Advancement of Science, 2017. https://doi.org/10.1126/science.aam5488.
ieee: F. M. Praetorius and H. Dietz, “Self-assembly of genetically encoded DNA-protein
hybrid nanoscale shapes,” Science, vol. 355, no. 6331. American Association
for the Advancement of Science, 2017.
ista: Praetorius FM, Dietz H. 2017. Self-assembly of genetically encoded DNA-protein
hybrid nanoscale shapes. Science. 355(6331), eaam5488.
mla: Praetorius, Florian M., and Hendrik Dietz. “Self-Assembly of Genetically Encoded
DNA-Protein Hybrid Nanoscale Shapes.” Science, vol. 355, no. 6331, eaam5488,
American Association for the Advancement of Science, 2017, doi:10.1126/science.aam5488.
short: F.M. Praetorius, H. Dietz, Science 355 (2017).
date_created: 2023-09-06T12:08:55Z
date_published: 2017-03-24T00:00:00Z
date_updated: 2023-11-07T12:33:05Z
day: '24'
doi: 10.1126/science.aam5488
extern: '1'
external_id:
pmid:
- '28336611'
intvolume: ' 355'
issue: '6331'
language:
- iso: eng
month: '03'
oa_version: None
pmid: 1
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Self-assembly of genetically encoded DNA-protein hybrid nanoscale shapes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 355
year: '2017'
...
---
_id: '14290'
abstract:
- lang: eng
text: DNA nanotechnology, in particular DNA origami, enables the bottom-up self-assembly
of micrometre-scale, three-dimensional structures with nanometre-precise features1,2,3,4,5,6,7,8,9,10,11,12.
These structures are customizable in that they can be site-specifically functionalized13
or constructed to exhibit machine-like14,15 or logic-gating behaviour16. Their
use has been limited to applications that require only small amounts of material
(of the order of micrograms), owing to the limitations of current production methods.
But many proposed applications, for example as therapeutic agents or in complex
materials3,16,17,18,19,20,21,22, could be realized if more material could be used.
In DNA origami, a nanostructure is assembled from a very long single-stranded
scaffold molecule held in place by many short single-stranded staple oligonucleotides.
Only the bacteriophage-derived scaffold molecules are amenable to scalable and
efficient mass production23; the shorter staple strands are obtained through costly
solid-phase synthesis24 or enzymatic processes25. Here we show that single strands
of DNA of virtually arbitrary length and with virtually arbitrary sequences can
be produced in a scalable and cost-efficient manner by using bacteriophages to
generate single-stranded precursor DNA that contains target strand sequences interleaved
with self-excising ‘cassettes’, with each cassette comprising two Zn2+-dependent
DNA-cleaving DNA enzymes. We produce all of the necessary single strands of DNA
for several DNA origami using shaker-flask cultures, and demonstrate end-to-end
production of macroscopic amounts of a DNA origami nanorod in a litre-scale stirred-tank
bioreactor. Our method is compatible with existing DNA origami design frameworks
and retains the modularity and addressability of DNA origami objects that are
necessary for implementing custom modifications using functional groups. With
all of the production and purification steps amenable to scaling, we expect that
our method will expand the scope of DNA nanotechnology in many areas of science
and technology.
article_processing_charge: No
article_type: original
author:
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Benjamin
full_name: Kick, Benjamin
last_name: Kick
- first_name: Karl L.
full_name: Behler, Karl L.
last_name: Behler
- first_name: Maximilian N.
full_name: Honemann, Maximilian N.
last_name: Honemann
- first_name: Dirk
full_name: Weuster-Botz, Dirk
last_name: Weuster-Botz
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
citation:
ama: Praetorius FM, Kick B, Behler KL, Honemann MN, Weuster-Botz D, Dietz H. Biotechnological
mass production of DNA origami. Nature. 2017;552(7683):84-87. doi:10.1038/nature24650
apa: Praetorius, F. M., Kick, B., Behler, K. L., Honemann, M. N., Weuster-Botz,
D., & Dietz, H. (2017). Biotechnological mass production of DNA origami. Nature.
Springer Nature. https://doi.org/10.1038/nature24650
chicago: Praetorius, Florian M, Benjamin Kick, Karl L. Behler, Maximilian N. Honemann,
Dirk Weuster-Botz, and Hendrik Dietz. “Biotechnological Mass Production of DNA
Origami.” Nature. Springer Nature, 2017. https://doi.org/10.1038/nature24650.
ieee: F. M. Praetorius, B. Kick, K. L. Behler, M. N. Honemann, D. Weuster-Botz,
and H. Dietz, “Biotechnological mass production of DNA origami,” Nature,
vol. 552, no. 7683. Springer Nature, pp. 84–87, 2017.
ista: Praetorius FM, Kick B, Behler KL, Honemann MN, Weuster-Botz D, Dietz H. 2017.
Biotechnological mass production of DNA origami. Nature. 552(7683), 84–87.
mla: Praetorius, Florian M., et al. “Biotechnological Mass Production of DNA Origami.”
Nature, vol. 552, no. 7683, Springer Nature, 2017, pp. 84–87, doi:10.1038/nature24650.
short: F.M. Praetorius, B. Kick, K.L. Behler, M.N. Honemann, D. Weuster-Botz, H.
Dietz, Nature 552 (2017) 84–87.
date_created: 2023-09-06T12:14:20Z
date_published: 2017-12-07T00:00:00Z
date_updated: 2023-11-07T12:24:49Z
day: '07'
doi: 10.1038/nature24650
extern: '1'
external_id:
pmid:
- '29219963'
intvolume: ' 552'
issue: '7683'
language:
- iso: eng
month: '12'
oa_version: None
page: 84-87
pmid: 1
publication: Nature
publication_identifier:
eissn:
- 1476-4687
issn:
- 0028-0836
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Biotechnological mass production of DNA origami
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 552
year: '2017'
...
---
_id: '14308'
abstract:
- lang: eng
text: Here we describe an approach to bottom-up fabrication with nanometer-precision
that allows integrating the functional diversity of proteins in designed three-dimensional
structural frameworks. We reimagined the successful DNA origami design principle
using a set of custom staple proteins to fold a double-stranded DNA template into
a user-defined shape. Each staple protein recognizes two distinct double-helical
DNA sequences and can carry additional functionalities. The staple proteins we
present here are based on the transcription activator-like (TAL) effector proteins.
Due to their repetitive structure these proteins offer a unique programmability
that enables us to construct numerous staple proteins targeting any desired DNA
sequence. Our approach is general, meaning that many different objects may be
created using the same set of rules, and it is modular, because components can
be modified or exchanged individually. We present rules for constructing megadalton-scale
DNA-protein hybrid nanostructures; introduce important structural motifs, such
as curvature, corners, and vertices; describe principles for creating multi-layer
DNA-protein objects with enhanced rigidity; and demonstrate the possibility to
combine our DNA-protein hybrid origami with conventional DNA nanotechnology. Since
all components can be encoded genetically, our structures should be amenable to
biotechnological mass-production. Moreover, since the target objects can self-assemble
at room temperature in near-physiological buffer, our hybrid origami may also
provide an attractive method to realize positioning and scaffolding tasks in vivo.
We expect our method to find application both in scaffolding protein functionalities
and in manipulating the spatial arrangement of genomic DNA.
article_number: 25a
article_processing_charge: No
article_type: original
author:
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
citation:
ama: Praetorius FM, Dietz H. Genetically encoded DNA-protein hybrid origami. Biophysical
Journal. 2017;112(3). doi:10.1016/j.bpj.2016.11.171
apa: Praetorius, F. M., & Dietz, H. (2017). Genetically encoded DNA-protein
hybrid origami. Biophysical Journal. Elsevier. https://doi.org/10.1016/j.bpj.2016.11.171
chicago: Praetorius, Florian M, and Hendrik Dietz. “Genetically Encoded DNA-Protein
Hybrid Origami.” Biophysical Journal. Elsevier, 2017. https://doi.org/10.1016/j.bpj.2016.11.171.
ieee: F. M. Praetorius and H. Dietz, “Genetically encoded DNA-protein hybrid origami,”
Biophysical Journal, vol. 112, no. 3. Elsevier, 2017.
ista: Praetorius FM, Dietz H. 2017. Genetically encoded DNA-protein hybrid origami.
Biophysical Journal. 112(3), 25a.
mla: Praetorius, Florian M., and Hendrik Dietz. “Genetically Encoded DNA-Protein
Hybrid Origami.” Biophysical Journal, vol. 112, no. 3, 25a, Elsevier, 2017,
doi:10.1016/j.bpj.2016.11.171.
short: F.M. Praetorius, H. Dietz, Biophysical Journal 112 (2017).
date_created: 2023-09-06T13:19:10Z
date_published: 2017-02-03T00:00:00Z
date_updated: 2023-11-07T11:28:58Z
day: '03'
doi: 10.1016/j.bpj.2016.11.171
extern: '1'
intvolume: ' 112'
issue: '3'
keyword:
- Biophysics
language:
- iso: eng
month: '02'
oa_version: None
publication: Biophysical Journal
publication_identifier:
issn:
- 0006-3495
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Genetically encoded DNA-protein hybrid origami
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 112
year: '2017'
...
---
_id: '14309'
abstract:
- lang: eng
text: Establishing precise control over the shape and the interactions of the microscopic
building blocks is essential for design of macroscopic soft materials with novel
structural, optical and mechanical properties. Here, we demonstrate robust assembly
of DNA origami filaments into cholesteric liquid crystals, one-dimensional supramolecular
twisted ribbons and two-dimensional colloidal membranes. The exquisite control
afforded by the DNA origami technology establishes a quantitative relationship
between the microscopic filament structure and the macroscopic cholesteric pitch.
Furthermore, it also enables robust assembly of one-dimensional twisted ribbons,
which behave as effective supramolecular polymers whose structure and elastic
properties can be precisely tuned by controlling the geometry of the elemental
building blocks. Our results demonstrate the potential synergy between DNA origami
technology and colloidal science, in which the former allows for rapid and robust
synthesis of complex particles, and the latter can be used to assemble such particles
into bulk materials.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: M
full_name: Siavashpouri, M
last_name: Siavashpouri
- first_name: CH
full_name: Wachauf, CH
last_name: Wachauf
- first_name: MJ
full_name: Zakhary, MJ
last_name: Zakhary
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: H
full_name: Dietz, H
last_name: Dietz
- first_name: Z
full_name: Dogic, Z
last_name: Dogic
citation:
ama: Siavashpouri M, Wachauf C, Zakhary M, Praetorius FM, Dietz H, Dogic Z. Molecular
engineering of chiral colloidal liquid crystals using DNA origami. Nature Materials.
2017;16(8):849-856. doi:10.1038/nmat4909
apa: Siavashpouri, M., Wachauf, C., Zakhary, M., Praetorius, F. M., Dietz, H., &
Dogic, Z. (2017). Molecular engineering of chiral colloidal liquid crystals using
DNA origami. Nature Materials. Springer Nature. https://doi.org/10.1038/nmat4909
chicago: Siavashpouri, M, CH Wachauf, MJ Zakhary, Florian M Praetorius, H Dietz,
and Z Dogic. “Molecular Engineering of Chiral Colloidal Liquid Crystals Using
DNA Origami.” Nature Materials. Springer Nature, 2017. https://doi.org/10.1038/nmat4909.
ieee: M. Siavashpouri, C. Wachauf, M. Zakhary, F. M. Praetorius, H. Dietz, and Z.
Dogic, “Molecular engineering of chiral colloidal liquid crystals using DNA origami,”
Nature Materials, vol. 16, no. 8. Springer Nature, pp. 849–856, 2017.
ista: Siavashpouri M, Wachauf C, Zakhary M, Praetorius FM, Dietz H, Dogic Z. 2017.
Molecular engineering of chiral colloidal liquid crystals using DNA origami. Nature
Materials. 16(8), 849–856.
mla: Siavashpouri, M., et al. “Molecular Engineering of Chiral Colloidal Liquid
Crystals Using DNA Origami.” Nature Materials, vol. 16, no. 8, Springer
Nature, 2017, pp. 849–56, doi:10.1038/nmat4909.
short: M. Siavashpouri, C. Wachauf, M. Zakhary, F.M. Praetorius, H. Dietz, Z. Dogic,
Nature Materials 16 (2017) 849–856.
date_created: 2023-09-06T13:37:27Z
date_published: 2017-05-22T00:00:00Z
date_updated: 2023-11-07T11:40:00Z
day: '22'
doi: 10.1038/nmat4909
extern: '1'
external_id:
arxiv:
- '1705.08944'
pmid:
- '28530665'
intvolume: ' 16'
issue: '8'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: ' https://doi.org/10.48550/arXiv.1705.08944'
month: '05'
oa: 1
oa_version: Preprint
page: 849-856
pmid: 1
publication: Nature Materials
publication_identifier:
eissn:
- 1476-4660
issn:
- 1476-1122
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Molecular engineering of chiral colloidal liquid crystals using DNA origami
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 16
year: '2017'
...
---
_id: '14302'
abstract:
- lang: eng
text: One key goal of DNA nanotechnology is the bottom-up construction of macroscopic
crystalline materials. Beyond applications in fields such as photonics or plasmonics,
DNA-based crystal matrices could possibly facilitate the diffraction-based structural
analysis of guest molecules. Seeman and co-workers reported in 2009 the first
designed crystal matrices based on a 38 kDa DNA triangle that was composed of
seven chains. The crystal lattice was stabilized, unprecedentedly, by Watson–Crick
base pairing. However, 3D crystallization of larger designed DNA objects that
include more chains such as DNA origami remains an unsolved problem. Larger objects
would offer more degrees of freedom and design options with respect to tailoring
lattice geometry and for positioning other objects within a crystal lattice. The
greater rigidity of multilayer DNA origami could also positively influence the
diffractive properties of crystals composed of such particles. Here, we rationally
explore the role of heterogeneity and Watson–Crick interaction strengths in crystal
growth using 40 variants of the original DNA triangle as model multichain objects.
Crystal growth of the triangle was remarkably robust despite massive chemical,
geometrical, and thermodynamical sample heterogeneity that we introduced, but
the crystal growth sensitively depended on the sequences of base pairs next to
the Watson–Crick sticky ends of the triangle. Our results point to weak lattice
interactions and high concentrations as decisive factors for achieving productive
crystallization, while sample heterogeneity and impurities played a minor role.
article_processing_charge: No
article_type: original
author:
- first_name: Evi
full_name: Stahl, Evi
last_name: Stahl
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Carina C.
full_name: de Oliveira Mann, Carina C.
last_name: de Oliveira Mann
- first_name: Karl-Peter
full_name: Hopfner, Karl-Peter
last_name: Hopfner
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
citation:
ama: Stahl E, Praetorius FM, de Oliveira Mann CC, Hopfner K-P, Dietz H. Impact of
heterogeneity and lattice bond strength on DNA triangle crystal growth. ACS
Nano. 2016;10(10):9156-9164. doi:10.1021/acsnano.6b04787
apa: Stahl, E., Praetorius, F. M., de Oliveira Mann, C. C., Hopfner, K.-P., &
Dietz, H. (2016). Impact of heterogeneity and lattice bond strength on DNA triangle
crystal growth. ACS Nano. American Chemical Society. https://doi.org/10.1021/acsnano.6b04787
chicago: Stahl, Evi, Florian M Praetorius, Carina C. de Oliveira Mann, Karl-Peter
Hopfner, and Hendrik Dietz. “Impact of Heterogeneity and Lattice Bond Strength
on DNA Triangle Crystal Growth.” ACS Nano. American Chemical Society, 2016.
https://doi.org/10.1021/acsnano.6b04787.
ieee: E. Stahl, F. M. Praetorius, C. C. de Oliveira Mann, K.-P. Hopfner, and H.
Dietz, “Impact of heterogeneity and lattice bond strength on DNA triangle crystal
growth,” ACS Nano, vol. 10, no. 10. American Chemical Society, pp. 9156–9164,
2016.
ista: Stahl E, Praetorius FM, de Oliveira Mann CC, Hopfner K-P, Dietz H. 2016. Impact
of heterogeneity and lattice bond strength on DNA triangle crystal growth. ACS
Nano. 10(10), 9156–9164.
mla: Stahl, Evi, et al. “Impact of Heterogeneity and Lattice Bond Strength on DNA
Triangle Crystal Growth.” ACS Nano, vol. 10, no. 10, American Chemical
Society, 2016, pp. 9156–64, doi:10.1021/acsnano.6b04787.
short: E. Stahl, F.M. Praetorius, C.C. de Oliveira Mann, K.-P. Hopfner, H. Dietz,
ACS Nano 10 (2016) 9156–9164.
date_created: 2023-09-06T12:52:00Z
date_published: 2016-09-01T00:00:00Z
date_updated: 2023-11-07T12:08:46Z
day: '01'
doi: 10.1021/acsnano.6b04787
extern: '1'
external_id:
pmid:
- '27583560'
intvolume: ' 10'
issue: '10'
language:
- iso: eng
month: '09'
oa_version: None
page: 9156-9164
pmid: 1
publication: ACS Nano
publication_identifier:
eissn:
- 1936-086X
issn:
- 1936-0851
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Impact of heterogeneity and lattice bond strength on DNA triangle crystal growth
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 10
year: '2016'
...
---
_id: '14304'
abstract:
- lang: eng
text: Despite the recent rapid progress in cryo-electron microscopy (cryo-EM), there
still exist ample opportunities for improvement in sample preparation. Macromolecular
complexes may disassociate or adopt nonrandom orientations against the extended
air–water interface that exists for a short time before the sample is frozen.
We designed a hollow support structure using 3D DNA origami to protect complexes
from the detrimental effects of cryo-EM sample preparation. For a first proof-of-principle,
we concentrated on the transcription factor p53, which binds to specific DNA sequences
on double-stranded DNA. The support structures spontaneously form monolayers of
preoriented particles in a thin film of water, and offer advantages in particle
picking and sorting. By controlling the position of the binding sequence on a
single helix that spans the hollow support structure, we also sought to control
the orientation of individual p53 complexes. Although the latter did not yet yield
the desired results, the support structures did provide partial information about
the relative orientations of individual p53 complexes. We used this information
to calculate a tomographic 3D reconstruction, and refined this structure to a
final resolution of ∼15 Å. This structure settles an ongoing debate about the
symmetry of the p53 tetramer bound to DNA.
article_processing_charge: No
article_type: original
author:
- first_name: Thomas G.
full_name: Martin, Thomas G.
last_name: Martin
- first_name: Tanmay A. M.
full_name: Bharat, Tanmay A. M.
last_name: Bharat
- first_name: Andreas C.
full_name: Joerger, Andreas C.
last_name: Joerger
- first_name: Xiao-chen
full_name: Bai, Xiao-chen
last_name: Bai
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Alan R.
full_name: Fersht, Alan R.
last_name: Fersht
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
- first_name: Sjors H. W.
full_name: Scheres, Sjors H. W.
last_name: Scheres
citation:
ama: Martin TG, Bharat TAM, Joerger AC, et al. Design of a molecular support for
cryo-EM structure determination. PNAS. 2016;113(47):E7456-E7463. doi:10.1073/pnas.1612720113
apa: Martin, T. G., Bharat, T. A. M., Joerger, A. C., Bai, X., Praetorius, F. M.,
Fersht, A. R., … Scheres, S. H. W. (2016). Design of a molecular support for cryo-EM
structure determination. PNAS. Proceedings of the National Academy of Sciences.
https://doi.org/10.1073/pnas.1612720113
chicago: Martin, Thomas G., Tanmay A. M. Bharat, Andreas C. Joerger, Xiao-chen Bai,
Florian M Praetorius, Alan R. Fersht, Hendrik Dietz, and Sjors H. W. Scheres.
“Design of a Molecular Support for Cryo-EM Structure Determination.” PNAS.
Proceedings of the National Academy of Sciences, 2016. https://doi.org/10.1073/pnas.1612720113.
ieee: T. G. Martin et al., “Design of a molecular support for cryo-EM structure
determination,” PNAS, vol. 113, no. 47. Proceedings of the National Academy
of Sciences, pp. E7456–E7463, 2016.
ista: Martin TG, Bharat TAM, Joerger AC, Bai X, Praetorius FM, Fersht AR, Dietz
H, Scheres SHW. 2016. Design of a molecular support for cryo-EM structure determination.
PNAS. 113(47), E7456–E7463.
mla: Martin, Thomas G., et al. “Design of a Molecular Support for Cryo-EM Structure
Determination.” PNAS, vol. 113, no. 47, Proceedings of the National Academy
of Sciences, 2016, pp. E7456–63, doi:10.1073/pnas.1612720113.
short: T.G. Martin, T.A.M. Bharat, A.C. Joerger, X. Bai, F.M. Praetorius, A.R. Fersht,
H. Dietz, S.H.W. Scheres, PNAS 113 (2016) E7456–E7463.
date_created: 2023-09-06T12:53:48Z
date_published: 2016-10-13T00:00:00Z
date_updated: 2023-11-07T11:53:06Z
day: '13'
doi: 10.1073/pnas.1612720113
extern: '1'
external_id:
pmid:
- '27821763'
intvolume: ' 113'
issue: '47'
language:
- iso: eng
month: '10'
oa_version: Published Version
page: E7456-E7463
pmid: 1
publication: PNAS
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Design of a molecular support for cryo-EM structure determination
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 113
year: '2016'
...
---
_id: '14303'
abstract:
- lang: eng
text: Scaffolded DNA origami enables the fabrication of a variety of complex nanostructures
that promise utility in diverse fields of application, ranging from biosensing
over advanced therapeutics to metamaterials. The broad applicability of DNA origami
as a material beyond the level of proof-of-concept studies critically depends,
among other factors, on the availability of large amounts of pure single-stranded
scaffold DNA. Here, we present a method for the efficient production of M13 bacteriophage-derived
genomic DNA using high-cell-density fermentation of Escherichia coli in stirred-tank
bioreactors. We achieve phage titers of up to 1.6 × 1014 plaque-forming units
per mL. Downstream processing yields up to 410 mg of high-quality single-stranded
DNA per one liter reaction volume, thus upgrading DNA origami-based nanotechnology
from the milligram to the gram scale.
article_processing_charge: No
article_type: letter_note
author:
- first_name: B
full_name: Kick, B
last_name: Kick
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: H
full_name: Dietz, H
last_name: Dietz
- first_name: D
full_name: Weuster-Botz, D
last_name: Weuster-Botz
citation:
ama: Kick B, Praetorius FM, Dietz H, Weuster-Botz D. Efficient production of single-stranded
phage DNA as scaffolds for DNA origami. Nano Letters. 2015;15(7):4672-4676.
doi:10.1021/acs.nanolett.5b01461
apa: Kick, B., Praetorius, F. M., Dietz, H., & Weuster-Botz, D. (2015). Efficient
production of single-stranded phage DNA as scaffolds for DNA origami. Nano
Letters. ACS Publications. https://doi.org/10.1021/acs.nanolett.5b01461
chicago: Kick, B, Florian M Praetorius, H Dietz, and D Weuster-Botz. “Efficient
Production of Single-Stranded Phage DNA as Scaffolds for DNA Origami.” Nano
Letters. ACS Publications, 2015. https://doi.org/10.1021/acs.nanolett.5b01461.
ieee: B. Kick, F. M. Praetorius, H. Dietz, and D. Weuster-Botz, “Efficient production
of single-stranded phage DNA as scaffolds for DNA origami,” Nano Letters,
vol. 15, no. 7. ACS Publications, pp. 4672–4676, 2015.
ista: Kick B, Praetorius FM, Dietz H, Weuster-Botz D. 2015. Efficient production
of single-stranded phage DNA as scaffolds for DNA origami. Nano Letters. 15(7),
4672–4676.
mla: Kick, B., et al. “Efficient Production of Single-Stranded Phage DNA as Scaffolds
for DNA Origami.” Nano Letters, vol. 15, no. 7, ACS Publications, 2015,
pp. 4672–76, doi:10.1021/acs.nanolett.5b01461.
short: B. Kick, F.M. Praetorius, H. Dietz, D. Weuster-Botz, Nano Letters 15 (2015)
4672–4676.
date_created: 2023-09-06T12:52:47Z
date_published: 2015-06-01T00:00:00Z
date_updated: 2023-11-07T11:56:32Z
day: '01'
doi: 10.1021/acs.nanolett.5b01461
extern: '1'
external_id:
pmid:
- '26028443'
intvolume: ' 15'
issue: '7'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1021/acs.nanolett.5b01461
month: '06'
oa: 1
oa_version: Published Version
page: 4672-4676
pmid: 1
publication: Nano Letters
publication_identifier:
eissn:
- 1530-6992
issn:
- 1530-6984
publication_status: published
publisher: ACS Publications
quality_controlled: '1'
status: public
title: Efficient production of single-stranded phage DNA as scaffolds for DNA origami
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 15
year: '2015'
...
---
_id: '14301'
abstract:
- lang: eng
text: DNA has become a prime material for assembling complex three-dimensional objects
that promise utility in various areas of application. However, achieving user-defined
goals with DNA objects has been hampered by the difficulty to prepare them at
arbitrary concentrations and in user-defined solution conditions. Here, we describe
a method that solves this problem. The method is based on poly(ethylene glycol)-induced
depletion of species with high molecular weight. We demonstrate that our method
is applicable to a wide spectrum of DNA shapes and that it achieves excellent
recovery yields of target objects up to 97 %, while providing efficient separation
from non-integrated DNA strands. DNA objects may be prepared at concentrations
up to the limit of solubility, including the possibility for bringing DNA objects
into a solid phase. Due to the fidelity and simplicity of our method we anticipate
that it will help to catalyze the development of new types of applications that
use self-assembled DNA objects.
article_processing_charge: No
article_type: original
author:
- first_name: Evi
full_name: Stahl, Evi
last_name: Stahl
- first_name: Thomas
full_name: Martin, Thomas
last_name: Martin
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Hendrik
full_name: Dietz, Hendrik
last_name: Dietz
citation:
ama: Stahl E, Martin T, Praetorius FM, Dietz H. Facile and scalable preparation
of pure and dense DNA origami solutions. Angewandte Chemie International Edition.
2014;126(47):12949-12954. doi:10.1002/ange.201405991
apa: Stahl, E., Martin, T., Praetorius, F. M., & Dietz, H. (2014). Facile and
scalable preparation of pure and dense DNA origami solutions. Angewandte Chemie
International Edition. Wiley. https://doi.org/10.1002/ange.201405991
chicago: Stahl, Evi, Thomas Martin, Florian M Praetorius, and Hendrik Dietz. “Facile
and Scalable Preparation of Pure and Dense DNA Origami Solutions.” Angewandte
Chemie International Edition. Wiley, 2014. https://doi.org/10.1002/ange.201405991.
ieee: E. Stahl, T. Martin, F. M. Praetorius, and H. Dietz, “Facile and scalable
preparation of pure and dense DNA origami solutions,” Angewandte Chemie International
Edition, vol. 126, no. 47. Wiley, pp. 12949–12954, 2014.
ista: Stahl E, Martin T, Praetorius FM, Dietz H. 2014. Facile and scalable preparation
of pure and dense DNA origami solutions. Angewandte Chemie International Edition.
126(47), 12949–12954.
mla: Stahl, Evi, et al. “Facile and Scalable Preparation of Pure and Dense DNA Origami
Solutions.” Angewandte Chemie International Edition, vol. 126, no. 47,
Wiley, 2014, pp. 12949–54, doi:10.1002/ange.201405991.
short: E. Stahl, T. Martin, F.M. Praetorius, H. Dietz, Angewandte Chemie International
Edition 126 (2014) 12949–12954.
date_created: 2023-09-06T12:51:14Z
date_published: 2014-11-17T00:00:00Z
date_updated: 2023-11-07T12:14:30Z
day: '17'
doi: 10.1002/ange.201405991
extern: '1'
external_id:
pmid:
- '25346175'
intvolume: ' 126'
issue: '47'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/ange.201405991
month: '11'
oa: 1
oa_version: Published Version
page: 12949-12954
pmid: 1
publication: Angewandte Chemie International Edition
publication_identifier:
eissn:
- 1521-3773
issn:
- 1433-7851
publication_status: published
publisher: Wiley
quality_controlled: '1'
scopus_import: '1'
status: public
title: Facile and scalable preparation of pure and dense DNA origami solutions
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 126
year: '2014'
...
---
_id: '14305'
abstract:
- lang: eng
text: Understanding the mechanism of protein folding requires a detailed knowledge
of the structural properties of the barriers separating unfolded from native conformations.
The S-peptide from ribonuclease S forms its α-helical structure only upon binding
to the folded S-protein. We characterized the transition state for this binding-induced
folding reaction at high resolution by determining the effect of site-specific
backbone thioxylation and side-chain modifications on the kinetics and thermodynamics
of the reaction, which allows us to monitor formation of backbone hydrogen bonds
and side-chain interactions in the transition state. The experiments reveal that
α-helical structure in the S-peptide is absent in the transition state of binding.
Recognition between the unfolded S-peptide and the S-protein is mediated by loosely
packed hydrophobic side-chain interactions in two well defined regions on the
S-peptide. Close packing and helix formation occurs rapidly after binding. Introducing
hydrophobic residues at positions outside the recognition region can drastically
slow down association.
article_processing_charge: No
article_type: original
author:
- first_name: Annett
full_name: Bachmann, Annett
last_name: Bachmann
- first_name: Dirk
full_name: Wildemann, Dirk
last_name: Wildemann
- first_name: Florian M
full_name: Praetorius, Florian M
id: dfec9381-4341-11ee-8fd8-faa02bba7d62
last_name: Praetorius
- first_name: Gunter
full_name: Fischer, Gunter
last_name: Fischer
- first_name: Thomas
full_name: Kiefhaber, Thomas
last_name: Kiefhaber
citation:
ama: Bachmann A, Wildemann D, Praetorius FM, Fischer G, Kiefhaber T. Mapping backbone
and side-chain interactions in the transition state of a coupled protein folding
and binding reaction. PNAS. 2011;108(10):3952-3957. doi:10.1073/pnas.1012668108
apa: Bachmann, A., Wildemann, D., Praetorius, F. M., Fischer, G., & Kiefhaber,
T. (2011). Mapping backbone and side-chain interactions in the transition state
of a coupled protein folding and binding reaction. PNAS. Proceedings of
the National Academy of Sciences. https://doi.org/10.1073/pnas.1012668108
chicago: Bachmann, Annett, Dirk Wildemann, Florian M Praetorius, Gunter Fischer,
and Thomas Kiefhaber. “Mapping Backbone and Side-Chain Interactions in the Transition
State of a Coupled Protein Folding and Binding Reaction.” PNAS. Proceedings
of the National Academy of Sciences, 2011. https://doi.org/10.1073/pnas.1012668108.
ieee: A. Bachmann, D. Wildemann, F. M. Praetorius, G. Fischer, and T. Kiefhaber,
“Mapping backbone and side-chain interactions in the transition state of a coupled
protein folding and binding reaction,” PNAS, vol. 108, no. 10. Proceedings
of the National Academy of Sciences, pp. 3952–3957, 2011.
ista: Bachmann A, Wildemann D, Praetorius FM, Fischer G, Kiefhaber T. 2011. Mapping
backbone and side-chain interactions in the transition state of a coupled protein
folding and binding reaction. PNAS. 108(10), 3952–3957.
mla: Bachmann, Annett, et al. “Mapping Backbone and Side-Chain Interactions in the
Transition State of a Coupled Protein Folding and Binding Reaction.” PNAS,
vol. 108, no. 10, Proceedings of the National Academy of Sciences, 2011, pp. 3952–57,
doi:10.1073/pnas.1012668108.
short: A. Bachmann, D. Wildemann, F.M. Praetorius, G. Fischer, T. Kiefhaber, PNAS
108 (2011) 3952–3957.
date_created: 2023-09-06T12:54:36Z
date_published: 2011-01-12T00:00:00Z
date_updated: 2023-11-07T11:50:29Z
day: '12'
doi: 10.1073/pnas.1012668108
extern: '1'
external_id:
pmid:
- '21325613'
intvolume: ' 108'
issue: '10'
keyword:
- Multidisciplinary
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1073/pnas.1012668108
month: '01'
oa: 1
oa_version: Published Version
page: 3952-3957
pmid: 1
publication: PNAS
publication_identifier:
eissn:
- 1091-6490
issn:
- 0027-8424
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Mapping backbone and side-chain interactions in the transition state of a coupled
protein folding and binding reaction
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 108
year: '2011'
...