---
_id: '8453'
abstract:
- lang: eng
  text: Transverse relaxation rate measurements in magic-angle spinning solid-state
    nuclear magnetic resonance provide information about molecular motions occurring
    on nanosecond-to-millisecond (ns–ms) time scales. The measurement of heteronuclear
    (13C, 15N) relaxation rate constants in the presence of a spin-lock radiofrequency
    field (R1ρ relaxation) provides access to such motions, and an increasing number
    of studies involving R1ρ relaxation in proteins have been reported. However, two
    factors that influence the observed relaxation rate constants have so far been
    neglected, namely, (1) the role of CSA/dipolar cross-correlated relaxation (CCR)
    and (2) the impact of fast proton spin flips (i.e., proton spin diffusion and
    relaxation). We show that CSA/D CCR in R1ρ experiments is measurable and that
    the CCR rate constant depends on ns–ms motions; it can thus provide insight into
    dynamics. We find that proton spin diffusion attenuates this CCR due to its decoupling
    effect on the doublet components. For measurements of dynamics, the use of R1ρ
    rate constants has practical advantages over the use of CCR rates, and this article
    reveals factors that have so far been disregarded and which are important for
    accurate measurements and interpretation.
article_processing_charge: No
article_type: original
author:
- first_name: Vilius
  full_name: Kurauskas, Vilius
  last_name: Kurauskas
- first_name: Emmanuelle
  full_name: Weber, Emmanuelle
  last_name: Weber
- first_name: Audrey
  full_name: Hessel, Audrey
  last_name: Hessel
- first_name: Isabel
  full_name: Ayala, Isabel
  last_name: Ayala
- first_name: Dominique
  full_name: Marion, Dominique
  last_name: Marion
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P. Cross-correlated
    relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning
    R1ρ NMR measurements: Application to protein backbone dynamics measurements. <i>The
    Journal of Physical Chemistry B</i>. 2016;120(34):8905-8913. doi:<a href="https://doi.org/10.1021/acs.jpcb.6b06129">10.1021/acs.jpcb.6b06129</a>'
  apa: 'Kurauskas, V., Weber, E., Hessel, A., Ayala, I., Marion, D., &#38; Schanda,
    P. (2016). Cross-correlated relaxation of dipolar coupling and chemical-shift
    anisotropy in magic-angle spinning R1ρ NMR measurements: Application to protein
    backbone dynamics measurements. <i>The Journal of Physical Chemistry B</i>. American
    Chemical Society. <a href="https://doi.org/10.1021/acs.jpcb.6b06129">https://doi.org/10.1021/acs.jpcb.6b06129</a>'
  chicago: 'Kurauskas, Vilius, Emmanuelle Weber, Audrey Hessel, Isabel Ayala, Dominique
    Marion, and Paul Schanda. “Cross-Correlated Relaxation of Dipolar Coupling and
    Chemical-Shift Anisotropy in Magic-Angle Spinning R1ρ NMR Measurements: Application
    to Protein Backbone Dynamics Measurements.” <i>The Journal of Physical Chemistry
    B</i>. American Chemical Society, 2016. <a href="https://doi.org/10.1021/acs.jpcb.6b06129">https://doi.org/10.1021/acs.jpcb.6b06129</a>.'
  ieee: 'V. Kurauskas, E. Weber, A. Hessel, I. Ayala, D. Marion, and P. Schanda, “Cross-correlated
    relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning
    R1ρ NMR measurements: Application to protein backbone dynamics measurements,”
    <i>The Journal of Physical Chemistry B</i>, vol. 120, no. 34. American Chemical
    Society, pp. 8905–8913, 2016.'
  ista: 'Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P. 2016. Cross-correlated
    relaxation of dipolar coupling and chemical-shift anisotropy in magic-angle spinning
    R1ρ NMR measurements: Application to protein backbone dynamics measurements. The
    Journal of Physical Chemistry B. 120(34), 8905–8913.'
  mla: 'Kurauskas, Vilius, et al. “Cross-Correlated Relaxation of Dipolar Coupling
    and Chemical-Shift Anisotropy in Magic-Angle Spinning R1ρ NMR Measurements: Application
    to Protein Backbone Dynamics Measurements.” <i>The Journal of Physical Chemistry
    B</i>, vol. 120, no. 34, American Chemical Society, 2016, pp. 8905–13, doi:<a
    href="https://doi.org/10.1021/acs.jpcb.6b06129">10.1021/acs.jpcb.6b06129</a>.'
  short: V. Kurauskas, E. Weber, A. Hessel, I. Ayala, D. Marion, P. Schanda, The Journal
    of Physical Chemistry B 120 (2016) 8905–8913.
date_created: 2020-09-18T10:07:07Z
date_published: 2016-08-08T00:00:00Z
date_updated: 2021-01-12T08:19:22Z
day: '08'
doi: 10.1021/acs.jpcb.6b06129
extern: '1'
intvolume: '       120'
issue: '34'
keyword:
- Physical and Theoretical Chemistry
- Materials Chemistry
- Surfaces
- Coatings and Films
language:
- iso: eng
month: '08'
oa_version: None
page: 8905-8913
publication: The Journal of Physical Chemistry B
publication_identifier:
  issn:
  - 1520-6106
  - 1520-5207
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: 'Cross-correlated relaxation of dipolar coupling and chemical-shift anisotropy
  in magic-angle spinning R1ρ NMR measurements: Application to protein backbone dynamics
  measurements'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 120
year: '2016'
...
---
_id: '7780'
abstract:
- lang: eng
  text: 'We used single-channel electrical recordings and Langevin molecular dynamics
    simulations to explore the electrophoretic translocation of various β-hairpin
    peptides across the staphylococcal α-hemolysin (αHL) protein pore at single-molecule
    resolution. The β-hairpin peptides, which varied in their folding properties,
    corresponded to the C terminal residues of the B1 domain of protein G. The translocation
    time was strongly dependent on the electric force and was correlated with the
    folding features of the β-hairpin peptides. Highly unfolded peptides entered the
    pore in an extended conformation, resulting in fast single-file translocation
    events. In contrast, the translocation of the folded β-hairpin peptides occurred
    more slowly. In this case, the β-hairpin peptides traversed the αHL pore in a
    misfolded or fully folded conformation. This study demonstrates that the interaction
    between a polypeptide and a β-barrel protein pore is dependent on the folding
    features of the polypeptide. '
article_processing_charge: No
article_type: original
author:
- first_name: Carl Peter
  full_name: Goodrich, Carl Peter
  id: EB352CD2-F68A-11E9-89C5-A432E6697425
  last_name: Goodrich
  orcid: 0000-0002-1307-5074
- first_name: Serdal
  full_name: Kirmizialtin, Serdal
  last_name: Kirmizialtin
- first_name: Beatrice M.
  full_name: Huyghues-Despointes, Beatrice M.
  last_name: Huyghues-Despointes
- first_name: Aiping
  full_name: Zhu, Aiping
  last_name: Zhu
- first_name: J. Martin
  full_name: Scholtz, J. Martin
  last_name: Scholtz
- first_name: Dmitrii E.
  full_name: Makarov, Dmitrii E.
  last_name: Makarov
- first_name: Liviu
  full_name: Movileanu, Liviu
  last_name: Movileanu
citation:
  ama: Goodrich CP, Kirmizialtin S, Huyghues-Despointes BM, et al. Single-molecule
    electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics
    simulations. <i>The Journal of Physical Chemistry B</i>. 2007;111(13):3332-3335.
    doi:<a href="https://doi.org/10.1021/jp071364h">10.1021/jp071364h</a>
  apa: Goodrich, C. P., Kirmizialtin, S., Huyghues-Despointes, B. M., Zhu, A., Scholtz,
    J. M., Makarov, D. E., &#38; Movileanu, L. (2007). Single-molecule electrophoresis
    of β-hairpin peptides by electrical recordings and Langevin dynamics simulations.
    <i>The Journal of Physical Chemistry B</i>. American Chemical Society. <a href="https://doi.org/10.1021/jp071364h">https://doi.org/10.1021/jp071364h</a>
  chicago: Goodrich, Carl Peter, Serdal Kirmizialtin, Beatrice M. Huyghues-Despointes,
    Aiping Zhu, J. Martin Scholtz, Dmitrii E. Makarov, and Liviu Movileanu. “Single-Molecule
    Electrophoresis of β-Hairpin Peptides by Electrical Recordings and Langevin Dynamics
    Simulations.” <i>The Journal of Physical Chemistry B</i>. American Chemical Society,
    2007. <a href="https://doi.org/10.1021/jp071364h">https://doi.org/10.1021/jp071364h</a>.
  ieee: C. P. Goodrich <i>et al.</i>, “Single-molecule electrophoresis of β-hairpin
    peptides by electrical recordings and Langevin dynamics simulations,” <i>The Journal
    of Physical Chemistry B</i>, vol. 111, no. 13. American Chemical Society, pp.
    3332–3335, 2007.
  ista: Goodrich CP, Kirmizialtin S, Huyghues-Despointes BM, Zhu A, Scholtz JM, Makarov
    DE, Movileanu L. 2007. Single-molecule electrophoresis of β-hairpin peptides by
    electrical recordings and Langevin dynamics simulations. The Journal of Physical
    Chemistry B. 111(13), 3332–3335.
  mla: Goodrich, Carl Peter, et al. “Single-Molecule Electrophoresis of β-Hairpin
    Peptides by Electrical Recordings and Langevin Dynamics Simulations.” <i>The Journal
    of Physical Chemistry B</i>, vol. 111, no. 13, American Chemical Society, 2007,
    pp. 3332–35, doi:<a href="https://doi.org/10.1021/jp071364h">10.1021/jp071364h</a>.
  short: C.P. Goodrich, S. Kirmizialtin, B.M. Huyghues-Despointes, A. Zhu, J.M. Scholtz,
    D.E. Makarov, L. Movileanu, The Journal of Physical Chemistry B 111 (2007) 3332–3335.
date_created: 2020-04-30T12:19:15Z
date_published: 2007-03-13T00:00:00Z
date_updated: 2021-01-12T08:15:29Z
day: '13'
doi: 10.1021/jp071364h
extern: '1'
intvolume: '       111'
issue: '13'
language:
- iso: eng
month: '03'
oa_version: None
page: 3332-3335
publication: The Journal of Physical Chemistry B
publication_identifier:
  issn:
  - 1520-6106
  - 1520-5207
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Single-molecule electrophoresis of β-hairpin peptides by electrical recordings
  and Langevin dynamics simulations
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 111
year: '2007'
...
---
_id: '13430'
abstract:
- lang: eng
  text: Dynamic self-assembly (DySA) processes occurring outside of thermodynamic
    equilibrium underlie many forms of adaptive and intellligent behaviors in natural
    systems. Relatively little, however, is known about the principles that govern
    DySA and the ways in which it can be extended to artificial ensembles. This article
    discusses recent advances in both the theory and the practice of nonequilibrium
    self-assembly. It is argued that a union of ideas from thermodynamics and dynamic
    systems' theory can provide a general description of DySA. In parallel, heuristic
    design rules can be used to construct DySA systems of increasing complexities
    based on a variety of suitable interactions/potentials on length scales from nanoscopic
    to macroscopic. Applications of these rules to magnetohydrodynamic DySA are also
    discussed.
article_processing_charge: No
article_type: original
author:
- first_name: Marcin
  full_name: Fialkowski, Marcin
  last_name: Fialkowski
- first_name: Kyle J. M.
  full_name: Bishop, Kyle J. M.
  last_name: Bishop
- first_name: Rafal
  full_name: Klajn, Rafal
  id: 8e84690e-1e48-11ed-a02b-a1e6fb8bb53b
  last_name: Klajn
- first_name: Stoyan K.
  full_name: Smoukov, Stoyan K.
  last_name: Smoukov
- first_name: Christopher J.
  full_name: Campbell, Christopher J.
  last_name: Campbell
- first_name: Bartosz A.
  full_name: Grzybowski, Bartosz A.
  last_name: Grzybowski
citation:
  ama: Fialkowski M, Bishop KJM, Klajn R, Smoukov SK, Campbell CJ, Grzybowski BA.
    Principles and implementations of dissipative (dynamic) self-assembly. <i>The
    Journal of Physical Chemistry B</i>. 2006;110(6):2482-2496. doi:<a href="https://doi.org/10.1021/jp054153q">10.1021/jp054153q</a>
  apa: Fialkowski, M., Bishop, K. J. M., Klajn, R., Smoukov, S. K., Campbell, C. J.,
    &#38; Grzybowski, B. A. (2006). Principles and implementations of dissipative
    (dynamic) self-assembly. <i>The Journal of Physical Chemistry B</i>. American
    Chemical Society. <a href="https://doi.org/10.1021/jp054153q">https://doi.org/10.1021/jp054153q</a>
  chicago: Fialkowski, Marcin, Kyle J. M. Bishop, Rafal Klajn, Stoyan K. Smoukov,
    Christopher J. Campbell, and Bartosz A. Grzybowski. “Principles and Implementations
    of Dissipative (Dynamic) Self-Assembly.” <i>The Journal of Physical Chemistry
    B</i>. American Chemical Society, 2006. <a href="https://doi.org/10.1021/jp054153q">https://doi.org/10.1021/jp054153q</a>.
  ieee: M. Fialkowski, K. J. M. Bishop, R. Klajn, S. K. Smoukov, C. J. Campbell, and
    B. A. Grzybowski, “Principles and implementations of dissipative (dynamic) self-assembly,”
    <i>The Journal of Physical Chemistry B</i>, vol. 110, no. 6. American Chemical
    Society, pp. 2482–2496, 2006.
  ista: Fialkowski M, Bishop KJM, Klajn R, Smoukov SK, Campbell CJ, Grzybowski BA.
    2006. Principles and implementations of dissipative (dynamic) self-assembly. The
    Journal of Physical Chemistry B. 110(6), 2482–2496.
  mla: Fialkowski, Marcin, et al. “Principles and Implementations of Dissipative (Dynamic)
    Self-Assembly.” <i>The Journal of Physical Chemistry B</i>, vol. 110, no. 6, American
    Chemical Society, 2006, pp. 2482–96, doi:<a href="https://doi.org/10.1021/jp054153q">10.1021/jp054153q</a>.
  short: M. Fialkowski, K.J.M. Bishop, R. Klajn, S.K. Smoukov, C.J. Campbell, B.A.
    Grzybowski, The Journal of Physical Chemistry B 110 (2006) 2482–2496.
date_created: 2023-08-01T10:37:35Z
date_published: 2006-01-25T00:00:00Z
date_updated: 2023-08-08T11:33:08Z
day: '25'
doi: 10.1021/jp054153q
extern: '1'
external_id:
  pmid:
  - '16471845'
intvolume: '       110'
issue: '6'
keyword:
- Materials Chemistry
- Surfaces
- Coatings and Films
- Physical and Theoretical Chemistry
language:
- iso: eng
month: '01'
oa_version: None
page: 2482-2496
pmid: 1
publication: The Journal of Physical Chemistry B
publication_identifier:
  issn:
  - 1520-6106
  - 1520-5207
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Principles and implementations of dissipative (dynamic) self-assembly
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 110
year: '2006'
...