[{"publication_identifier":{"issn":["1439-4235"]},"quality_controlled":"1","month":"01","volume":20,"article_type":"letter_note","pmid":1,"date_created":"2020-09-17T10:29:26Z","intvolume":"        20","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","extern":"1","_id":"8410","oa":1,"author":[{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul"},{"last_name":"Chekmenev","first_name":"Eduard Y.","full_name":"Chekmenev, Eduard Y."}],"date_published":"2019-01-21T00:00:00Z","year":"2019","publisher":"Wiley","doi":"10.1002/cphc.201801100","language":[{"iso":"eng"}],"type":"journal_article","main_file_link":[{"url":"https://doi.org/10.1002/cphc.201801100","open_access":"1"}],"title":"NMR for Biological Systems","external_id":{"pmid":["30556633"]},"publication":"ChemPhysChem","citation":{"ama":"Schanda P, Chekmenev EY. NMR for Biological Systems. <i>ChemPhysChem</i>. 2019;20(2):177-177. doi:<a href=\"https://doi.org/10.1002/cphc.201801100\">10.1002/cphc.201801100</a>","apa":"Schanda, P., &#38; Chekmenev, E. Y. (2019). NMR for Biological Systems. <i>ChemPhysChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cphc.201801100\">https://doi.org/10.1002/cphc.201801100</a>","mla":"Schanda, Paul, and Eduard Y. Chekmenev. “NMR for Biological Systems.” <i>ChemPhysChem</i>, vol. 20, no. 2, Wiley, 2019, pp. 177–177, doi:<a href=\"https://doi.org/10.1002/cphc.201801100\">10.1002/cphc.201801100</a>.","ista":"Schanda P, Chekmenev EY. 2019. NMR for Biological Systems. ChemPhysChem. 20(2), 177–177.","short":"P. Schanda, E.Y. Chekmenev, ChemPhysChem 20 (2019) 177–177.","ieee":"P. Schanda and E. Y. Chekmenev, “NMR for Biological Systems,” <i>ChemPhysChem</i>, vol. 20, no. 2. Wiley, pp. 177–177, 2019.","chicago":"Schanda, Paul, and Eduard Y. Chekmenev. “NMR for Biological Systems.” <i>ChemPhysChem</i>. Wiley, 2019. <a href=\"https://doi.org/10.1002/cphc.201801100\">https://doi.org/10.1002/cphc.201801100</a>."},"issue":"2","day":"21","oa_version":"Published Version","page":"177-177","publication_status":"published","date_updated":"2021-01-12T08:19:05Z","status":"public"},{"language":[{"iso":"eng"}],"doi":"10.1002/cphc.201800935","publisher":"Wiley","year":"2019","type":"journal_article","author":[{"full_name":"Marion, Dominique","first_name":"Dominique","last_name":"Marion"},{"full_name":"Gauto, Diego F.","first_name":"Diego F.","last_name":"Gauto"},{"full_name":"Ayala, Isabel","first_name":"Isabel","last_name":"Ayala"},{"last_name":"Giandoreggio-Barranco","first_name":"Karine","full_name":"Giandoreggio-Barranco, Karine"},{"full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"}],"_id":"8411","date_published":"2019-01-21T00:00:00Z","date_created":"2020-09-17T10:29:36Z","pmid":1,"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"intvolume":"        20","month":"01","quality_controlled":"1","publication_identifier":{"issn":["1439-4235"]},"article_type":"original","volume":20,"date_updated":"2021-01-12T08:19:06Z","status":"public","publication_status":"published","page":"276-284","oa_version":"Submitted Version","day":"21","abstract":[{"text":"Studying protein dynamics on microsecond‐to‐millisecond (μs‐ms) time scales can provide important insight into protein function. In magic‐angle‐spinning (MAS) NMR, μs dynamics can be visualized by R1p rotating‐frame relaxation dispersion experiments in different regimes of radio‐frequency field strengths: at low RF field strength, isotropic‐chemical‐shift fluctuation leads to “Bloch‐McConnell‐type” relaxation dispersion, while when the RF field approaches rotary resonance conditions bond angle fluctuations manifest as increased R1p rate constants (“Near‐Rotary‐Resonance Relaxation Dispersion”, NERRD). Here we explore the joint analysis of both regimes to gain comprehensive insight into motion in terms of geometric amplitudes, chemical‐shift changes, populations and exchange kinetics. We use a numerical simulation procedure to illustrate these effects and the potential of extracting exchange parameters, and apply the methodology to the study of a previously described conformational exchange process in microcrystalline ubiquitin.","lang":"eng"}],"citation":{"ieee":"D. Marion, D. F. Gauto, I. Ayala, K. Giandoreggio-Barranco, and P. Schanda, “Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR,” <i>ChemPhysChem</i>, vol. 20, no. 2. Wiley, pp. 276–284, 2019.","chicago":"Marion, Dominique, Diego F. Gauto, Isabel Ayala, Karine Giandoreggio-Barranco, and Paul Schanda. “Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance R1p Relaxation-Dispersion MAS NMR.” <i>ChemPhysChem</i>. Wiley, 2019. <a href=\"https://doi.org/10.1002/cphc.201800935\">https://doi.org/10.1002/cphc.201800935</a>.","ama":"Marion D, Gauto DF, Ayala I, Giandoreggio-Barranco K, Schanda P. Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR. <i>ChemPhysChem</i>. 2019;20(2):276-284. doi:<a href=\"https://doi.org/10.1002/cphc.201800935\">10.1002/cphc.201800935</a>","short":"D. Marion, D.F. Gauto, I. Ayala, K. Giandoreggio-Barranco, P. Schanda, ChemPhysChem 20 (2019) 276–284.","apa":"Marion, D., Gauto, D. F., Ayala, I., Giandoreggio-Barranco, K., &#38; Schanda, P. (2019). Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR. <i>ChemPhysChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cphc.201800935\">https://doi.org/10.1002/cphc.201800935</a>","mla":"Marion, Dominique, et al. “Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance R1p Relaxation-Dispersion MAS NMR.” <i>ChemPhysChem</i>, vol. 20, no. 2, Wiley, 2019, pp. 276–84, doi:<a href=\"https://doi.org/10.1002/cphc.201800935\">10.1002/cphc.201800935</a>.","ista":"Marion D, Gauto DF, Ayala I, Giandoreggio-Barranco K, Schanda P. 2019. Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR. ChemPhysChem. 20(2), 276–284."},"issue":"2","publication":"ChemPhysChem","external_id":{"pmid":["30444575"]},"title":"Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR"},{"citation":{"ama":"Shannon MD, Theint T, Mukhopadhyay D, et al. Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR. <i>ChemPhysChem</i>. 2019;20(2):311-317. doi:<a href=\"https://doi.org/10.1002/cphc.201800779\">10.1002/cphc.201800779</a>","mla":"Shannon, Matthew D., et al. “Conformational Dynamics in the Core of Human Y145Stop Prion Protein Amyloid Probed by Relaxation Dispersion NMR.” <i>ChemPhysChem</i>, vol. 20, no. 2, Wiley, 2019, pp. 311–17, doi:<a href=\"https://doi.org/10.1002/cphc.201800779\">10.1002/cphc.201800779</a>.","ista":"Shannon MD, Theint T, Mukhopadhyay D, Surewicz K, Surewicz WK, Marion D, Schanda P, Jaroniec CP. 2019. Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR. ChemPhysChem. 20(2), 311–317.","short":"M.D. Shannon, T. Theint, D. Mukhopadhyay, K. Surewicz, W.K. Surewicz, D. Marion, P. Schanda, C.P. Jaroniec, ChemPhysChem 20 (2019) 311–317.","apa":"Shannon, M. D., Theint, T., Mukhopadhyay, D., Surewicz, K., Surewicz, W. K., Marion, D., … Jaroniec, C. P. (2019). Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR. <i>ChemPhysChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cphc.201800779\">https://doi.org/10.1002/cphc.201800779</a>","ieee":"M. D. Shannon <i>et al.</i>, “Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR,” <i>ChemPhysChem</i>, vol. 20, no. 2. Wiley, pp. 311–317, 2019.","chicago":"Shannon, Matthew D., Theint Theint, Dwaipayan Mukhopadhyay, Krystyna Surewicz, Witold K. Surewicz, Dominique Marion, Paul Schanda, and Christopher P. Jaroniec. “Conformational Dynamics in the Core of Human Y145Stop Prion Protein Amyloid Probed by Relaxation Dispersion NMR.” <i>ChemPhysChem</i>. Wiley, 2019. <a href=\"https://doi.org/10.1002/cphc.201800779\">https://doi.org/10.1002/cphc.201800779</a>."},"issue":"2","external_id":{"pmid":["30276945"]},"title":"Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR","publication":"ChemPhysChem","date_updated":"2021-01-12T08:19:06Z","status":"public","abstract":[{"lang":"eng","text":"Microsecond to millisecond timescale backbone dynamics of the amyloid core residues in Y145Stop human prion protein (PrP) fibrils were investigated by using 15N rotating frame (R1ρ) relaxation dispersion solid‐state nuclear magnetic resonance spectroscopy over a wide range of spin‐lock fields. Numerical simulations enabled the experimental relaxation dispersion profiles for most of the fibril core residues to be modelled by using a two‐state exchange process with a common exchange rate of 1000 s−1, corresponding to protein backbone motion on the timescale of 1 ms, and an excited‐state population of 2 %. We also found that the relaxation dispersion profiles for several amino acids positioned near the edges of the most structured regions of the amyloid core were better modelled by assuming somewhat higher excited‐state populations (∼5–15 %) and faster exchange rate constants, corresponding to protein backbone motions on the timescale of ∼100–300 μs. The slow backbone dynamics of the core residues were evaluated in the context of the structural model of human Y145Stop PrP amyloid."}],"oa_version":"Submitted Version","publication_status":"published","page":"311-317","day":"21","pmid":1,"date_created":"2020-09-17T10:29:43Z","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"intvolume":"        20","article_processing_charge":"No","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","quality_controlled":"1","publication_identifier":{"issn":["1439-4235"]},"month":"01","article_type":"original","volume":20,"publisher":"Wiley","year":"2019","language":[{"iso":"eng"}],"doi":"10.1002/cphc.201800779","type":"journal_article","_id":"8412","author":[{"last_name":"Shannon","first_name":"Matthew D.","full_name":"Shannon, Matthew D."},{"last_name":"Theint","full_name":"Theint, Theint","first_name":"Theint"},{"last_name":"Mukhopadhyay","first_name":"Dwaipayan","full_name":"Mukhopadhyay, Dwaipayan"},{"first_name":"Krystyna","full_name":"Surewicz, Krystyna","last_name":"Surewicz"},{"last_name":"Surewicz","first_name":"Witold K.","full_name":"Surewicz, Witold K."},{"full_name":"Marion, Dominique","first_name":"Dominique","last_name":"Marion"},{"full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"},{"full_name":"Jaroniec, Christopher P.","first_name":"Christopher P.","last_name":"Jaroniec"}],"date_published":"2019-01-21T00:00:00Z"},{"keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"intvolume":"        18","issue":"19","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_processing_charge":"No","citation":{"chicago":"Fraga, Hugo, Charles‐Adrien Arnaud, Diego F. Gauto, Maxime Audin, Vilius Kurauskas, Pavel Macek, Carsten Krichel, et al. “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.” <i>ChemPhysChem</i>. Wiley, 2017. <a href=\"https://doi.org/10.1002/cphc.201700572\">https://doi.org/10.1002/cphc.201700572</a>.","ieee":"H. Fraga <i>et al.</i>, “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins,” <i>ChemPhysChem</i>, vol. 18, no. 19. Wiley, pp. 2697–2703, 2017.","short":"H. Fraga, C. Arnaud, D.F. Gauto, M. Audin, V. Kurauskas, P. Macek, C. Krichel, J. Guan, J. Boisbouvier, R. Sprangers, C. Breyton, P. Schanda, ChemPhysChem 18 (2017) 2697–2703.","apa":"Fraga, H., Arnaud, C., Gauto, D. F., Audin, M., Kurauskas, V., Macek, P., … Schanda, P. (2017). Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. <i>ChemPhysChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cphc.201700572\">https://doi.org/10.1002/cphc.201700572</a>","mla":"Fraga, Hugo, et al. “Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.” <i>ChemPhysChem</i>, vol. 18, no. 19, Wiley, 2017, pp. 2697–703, doi:<a href=\"https://doi.org/10.1002/cphc.201700572\">10.1002/cphc.201700572</a>.","ista":"Fraga H, Arnaud C, Gauto DF, Audin M, Kurauskas V, Macek P, Krichel C, Guan J, Boisbouvier J, Sprangers R, Breyton C, Schanda P. 2017. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. ChemPhysChem. 18(19), 2697–2703.","ama":"Fraga H, Arnaud C, Gauto DF, et al. Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins. <i>ChemPhysChem</i>. 2017;18(19):2697-2703. doi:<a href=\"https://doi.org/10.1002/cphc.201700572\">10.1002/cphc.201700572</a>"},"date_created":"2020-09-18T10:06:09Z","article_type":"original","volume":18,"title":"Solid‐state NMR H–N–(C)–H and H–N–C–C 3D/4D correlation experiments for resonance assignment of large proteins","publication":"ChemPhysChem","quality_controlled":"1","publication_identifier":{"issn":["1439-4235","1439-7641"]},"month":"08","type":"journal_article","status":"public","date_updated":"2021-01-12T08:19:19Z","publisher":"Wiley","year":"2017","language":[{"iso":"eng"}],"doi":"10.1002/cphc.201700572","abstract":[{"text":"Solid‐state NMR spectroscopy can provide insight into protein structure and dynamics at the atomic level without inherent protein size limitations. However, a major hurdle to studying large proteins by solid‐state NMR spectroscopy is related to spectral complexity and resonance overlap, which increase with molecular weight and severely hamper the assignment process. Here the use of two sets of experiments is shown to expand the tool kit of 1H‐detected assignment approaches, which correlate a given amide pair either to the two adjacent CO–CA pairs (4D hCOCANH/hCOCAcoNH), or to the amide 1H of the neighboring residue (3D HcocaNH/HcacoNH, which can be extended to 5D). The experiments are based on efficient coherence transfers between backbone atoms using INEPT transfers between carbons and cross‐polarization for heteronuclear transfers. The utility of these experiments is exemplified with application to assemblies of deuterated, fully amide‐protonated proteins from approximately 20 to 60 kDa monomer, at magic‐angle spinning (MAS) frequencies from approximately 40 to 55 kHz. These experiments will also be applicable to protonated proteins at higher MAS frequencies. The resonance assignment of a domain within the 50.4 kDa bacteriophage T5 tube protein pb6 is reported, and this is compared to NMR assignments of the isolated domain in solution. This comparison reveals contacts of this domain to the core of the polymeric tail tube assembly.","lang":"eng"}],"date_published":"2017-08-09T00:00:00Z","publication_status":"published","oa_version":"None","page":"2697-2703","day":"09","_id":"8446","author":[{"last_name":"Fraga","first_name":"Hugo","full_name":"Fraga, Hugo"},{"full_name":"Arnaud, Charles‐Adrien","first_name":"Charles‐Adrien","last_name":"Arnaud"},{"full_name":"Gauto, Diego F.","first_name":"Diego F.","last_name":"Gauto"},{"full_name":"Audin, Maxime","first_name":"Maxime","last_name":"Audin"},{"first_name":"Vilius","full_name":"Kurauskas, Vilius","last_name":"Kurauskas"},{"last_name":"Macek","full_name":"Macek, Pavel","first_name":"Pavel"},{"first_name":"Carsten","full_name":"Krichel, Carsten","last_name":"Krichel"},{"first_name":"Jia‐Ying","full_name":"Guan, Jia‐Ying","last_name":"Guan"},{"first_name":"Jerome","full_name":"Boisbouvier, Jerome","last_name":"Boisbouvier"},{"last_name":"Sprangers","first_name":"Remco","full_name":"Sprangers, Remco"},{"first_name":"Cécile","full_name":"Breyton, Cécile","last_name":"Breyton"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","orcid":"0000-0002-9350-7606","first_name":"Paul","full_name":"Schanda, Paul"}]},{"_id":"13388","oa":1,"author":[{"last_name":"Udayabhaskararao","first_name":"T.","full_name":"Udayabhaskararao, T."},{"full_name":"Kundu, Pintu K.","first_name":"Pintu K.","last_name":"Kundu"},{"full_name":"Ahrens, Johannes","first_name":"Johannes","last_name":"Ahrens"},{"first_name":"Rafal","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn"}],"date_published":"2016-06-17T00:00:00Z","year":"2016","publisher":"Wiley","doi":"10.1002/cphc.201600480","language":[{"iso":"eng"}],"type":"other_academic_publication","publication_identifier":{"issn":["1439-4235"],"eissn":["1439-7641"]},"quality_controlled":"1","month":"06","volume":17,"date_created":"2023-08-01T09:43:07Z","intvolume":"        17","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"article_processing_charge":"No","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","abstract":[{"text":"The Inside Cover picture illustrates the fluorescent properties of a gold nanocluster functionalized with several copies of a red-emitting merocyanine (image by Ella Marushchenko). The red fluorescence can be turned on and off reversibly by using an external stimulus.","lang":"eng"}],"day":"17","publication_status":"published","oa_version":"Published Version","page":"1711-1711","date_updated":"2023-08-07T12:43:38Z","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1002/cphc.201600480"}],"title":"Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016)","publication":"ChemPhysChem","citation":{"ieee":"T. Udayabhaskararao, P. K. Kundu, J. Ahrens, and R. Klajn, <i>Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016)</i>, vol. 17, no. 12. Wiley, 2016, pp. 1711–1711.","chicago":"Udayabhaskararao, T., Pintu K. Kundu, Johannes Ahrens, and Rafal Klajn. <i>Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016)</i>. <i>ChemPhysChem</i>. Vol. 17. Wiley, 2016. <a href=\"https://doi.org/10.1002/cphc.201600480\">https://doi.org/10.1002/cphc.201600480</a>.","ama":"Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. <i>Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016)</i>. Vol 17. Wiley; 2016:1711-1711. doi:<a href=\"https://doi.org/10.1002/cphc.201600480\">10.1002/cphc.201600480</a>","ista":"Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. 2016. Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016), Wiley,p.","apa":"Udayabhaskararao, T., Kundu, P. K., Ahrens, J., &#38; Klajn, R. (2016). <i>Inside cover: Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters (ChemPhysChem 12/2016)</i>. <i>ChemPhysChem</i> (Vol. 17, pp. 1711–1711). Wiley. <a href=\"https://doi.org/10.1002/cphc.201600480\">https://doi.org/10.1002/cphc.201600480</a>","short":"T. Udayabhaskararao, P.K. Kundu, J. Ahrens, R. Klajn, Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016), Wiley, 2016.","mla":"Udayabhaskararao, T., et al. “Inside Cover: Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters (ChemPhysChem 12/2016).” <i>ChemPhysChem</i>, vol. 17, no. 12, Wiley, 2016, pp. 1711–1711, doi:<a href=\"https://doi.org/10.1002/cphc.201600480\">10.1002/cphc.201600480</a>."},"issue":"12"},{"page":"1805-1809","publication_status":"published","oa_version":"None","day":"17","abstract":[{"lang":"eng","text":"Au25 nanoclusters functionalized with a spiropyran molecular switch are synthesized via a ligand-exchange reaction at low temperature. The resulting nanoclusters are characterized by optical and NMR spectroscopies as well as by mass spectrometry. Spiropyran bound to nanoclusters isomerizes in a reversible fashion when exposed to UV and visible light, and its properties are similar to those of free spiropyran molecules in solution. The reversible photoisomerization entails the modulation of fluorescence as well as the light-controlled self-assembly of nanoclusters."}],"status":"public","date_updated":"2023-08-07T12:46:46Z","publication":"ChemPhysChem","external_id":{"pmid":["26593975"]},"title":"Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters","issue":"12","scopus_import":"1","citation":{"chicago":"Udayabhaskararao, T., Pintu K. Kundu, Johannes Ahrens, and Rafal Klajn. “Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters.” <i>ChemPhysChem</i>. Wiley, 2016. <a href=\"https://doi.org/10.1002/cphc.201500897\">https://doi.org/10.1002/cphc.201500897</a>.","ieee":"T. Udayabhaskararao, P. K. Kundu, J. Ahrens, and R. Klajn, “Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters,” <i>ChemPhysChem</i>, vol. 17, no. 12. Wiley, pp. 1805–1809, 2016.","apa":"Udayabhaskararao, T., Kundu, P. K., Ahrens, J., &#38; Klajn, R. (2016). Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters. <i>ChemPhysChem</i>. Wiley. <a href=\"https://doi.org/10.1002/cphc.201500897\">https://doi.org/10.1002/cphc.201500897</a>","ista":"Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. 2016. Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters. ChemPhysChem. 17(12), 1805–1809.","short":"T. Udayabhaskararao, P.K. Kundu, J. Ahrens, R. Klajn, ChemPhysChem 17 (2016) 1805–1809.","mla":"Udayabhaskararao, T., et al. “Reversible Photoisomerization of Spiropyran on the Surfaces of Au25 Nanoclusters.” <i>ChemPhysChem</i>, vol. 17, no. 12, Wiley, 2016, pp. 1805–09, doi:<a href=\"https://doi.org/10.1002/cphc.201500897\">10.1002/cphc.201500897</a>.","ama":"Udayabhaskararao T, Kundu PK, Ahrens J, Klajn R. Reversible photoisomerization of spiropyran on the surfaces of Au25 nanoclusters. <i>ChemPhysChem</i>. 2016;17(12):1805-1809. doi:<a href=\"https://doi.org/10.1002/cphc.201500897\">10.1002/cphc.201500897</a>"},"date_published":"2016-06-17T00:00:00Z","author":[{"last_name":"Udayabhaskararao","first_name":"T.","full_name":"Udayabhaskararao, T."},{"full_name":"Kundu, Pintu K.","first_name":"Pintu K.","last_name":"Kundu"},{"last_name":"Ahrens","full_name":"Ahrens, Johannes","first_name":"Johannes"},{"full_name":"Klajn, Rafal","first_name":"Rafal","last_name":"Klajn","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"_id":"13389","type":"journal_article","language":[{"iso":"eng"}],"doi":"10.1002/cphc.201500897","publisher":"Wiley","year":"2016","article_type":"original","volume":17,"month":"06","quality_controlled":"1","publication_identifier":{"issn":["1439-4235"],"eissn":["1439-7641"]},"article_processing_charge":"No","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"intvolume":"        17","date_created":"2023-08-01T09:43:18Z","pmid":1},{"abstract":[{"text":"Adding a new dimension: 4D or 3D proton‐detected spectra of perdeuterated protein samples with 1H labelled amides and methyl groups permit collecting unambiguous distance restraints with high sensitivity and determining protein structure by solid‐state NMR (see picture).","lang":"eng"}],"day":"15","page":"915-918","publication_status":"published","oa_version":"None","date_published":"2011-02-15T00:00:00Z","_id":"8470","author":[{"last_name":"Huber","full_name":"Huber, Matthias","first_name":"Matthias"},{"full_name":"Hiller, Sebastian","first_name":"Sebastian","last_name":"Hiller"},{"full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"},{"last_name":"Ernst","full_name":"Ernst, Matthias","first_name":"Matthias"},{"full_name":"Böckmann, Anja","first_name":"Anja","last_name":"Böckmann"},{"full_name":"Verel, René","first_name":"René","last_name":"Verel"},{"full_name":"Meier, Beat H.","first_name":"Beat H.","last_name":"Meier"}],"type":"journal_article","status":"public","year":"2011","date_updated":"2021-01-12T08:19:30Z","publisher":"Wiley","doi":"10.1002/cphc.201100062","language":[{"iso":"eng"}],"title":"A proton-detected 4D solid-state NMR experiment for protein structure determination","volume":12,"article_type":"original","publication":"ChemPhysChem","publication_identifier":{"issn":["1439-4235"]},"quality_controlled":"1","month":"02","intvolume":"        12","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","issue":"5","article_processing_charge":"No","citation":{"chicago":"Huber, Matthias, Sebastian Hiller, Paul Schanda, Matthias Ernst, Anja Böckmann, René Verel, and Beat H. 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