[{"article_type":"original","citation":{"chicago":"Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin, Pavel Macek, Remy Sounier, Astrid C. Sivertsen, et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.” Nature Communications. Springer Nature, 2019. https://doi.org/10.1038/s41467-019-10490-9.","short":"D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier, A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A. Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019).","mla":"Gauto, Diego F., et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.” Nature Communications, vol. 10, 2697, Springer Nature, 2019, doi:10.1038/s41467-019-10490-9.","apa":"Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier, R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. Springer Nature. https://doi.org/10.1038/s41467-019-10490-9","ieee":"D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex,” Nature Communications, vol. 10. Springer Nature, 2019.","ista":"Gauto DF, Estrozi LF, Schwieters CD, Effantin G, Macek P, Sounier R, Sivertsen AC, Schmidt E, Kerfah R, Mas G, Colletier J-P, Güntert P, Favier A, Schoehn G, Schanda P, Boisbouvier J. 2019. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. 10, 2697.","ama":"Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex. Nature Communications. 2019;10. doi:10.1038/s41467-019-10490-9"},"publication":"Nature Communications","date_published":"2019-06-19T00:00:00Z","keyword":["General Biochemistry","Genetics and Molecular Biology","General Physics and Astronomy","General Chemistry"],"article_processing_charge":"No","day":"19","intvolume":" 10","title":"Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex","status":"public","_id":"8405","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Published Version","type":"journal_article","abstract":[{"lang":"eng","text":"Atomic-resolution structure determination is crucial for understanding protein function. Cryo-EM and NMR spectroscopy both provide structural information, but currently cryo-EM does not routinely give access to atomic-level structural data, and, generally, NMR structure determination is restricted to small (<30 kDa) proteins. We introduce an integrated structure determination approach that simultaneously uses NMR and EM data to overcome the limits of each of these methods. The approach enables structure determination of the 468 kDa large dodecameric aminopeptidase TET2 to a precision and accuracy below 1 Å by combining secondary-structure information obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large subunits, distance restraints from backbone amides and ILV methyl groups, and a 4.1 Å resolution EM map. The resulting structure exceeds current standards of NMR and EM structure determination in terms of molecular weight and precision. Importantly, the approach is successful even in cases where only medium-resolution cryo-EM data are available."}],"quality_controlled":"1","external_id":{"pmid":["31217444"]},"oa":1,"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41467-019-10490-9"}],"language":[{"iso":"eng"}],"doi":"10.1038/s41467-019-10490-9","publication_identifier":{"issn":["2041-1723"]},"month":"06","publisher":"Springer Nature","publication_status":"published","pmid":1,"year":"2019","volume":10,"date_created":"2020-09-17T10:28:25Z","date_updated":"2021-01-12T08:19:03Z","author":[{"full_name":"Gauto, Diego F.","last_name":"Gauto","first_name":"Diego F."},{"full_name":"Estrozi, Leandro F.","first_name":"Leandro F.","last_name":"Estrozi"},{"full_name":"Schwieters, Charles D.","last_name":"Schwieters","first_name":"Charles D."},{"first_name":"Gregory","last_name":"Effantin","full_name":"Effantin, Gregory"},{"last_name":"Macek","first_name":"Pavel","full_name":"Macek, Pavel"},{"first_name":"Remy","last_name":"Sounier","full_name":"Sounier, Remy"},{"last_name":"Sivertsen","first_name":"Astrid C.","full_name":"Sivertsen, Astrid C."},{"last_name":"Schmidt","first_name":"Elena","full_name":"Schmidt, Elena"},{"last_name":"Kerfah","first_name":"Rime","full_name":"Kerfah, Rime"},{"full_name":"Mas, Guillaume","first_name":"Guillaume","last_name":"Mas"},{"last_name":"Colletier","first_name":"Jacques-Philippe","full_name":"Colletier, Jacques-Philippe"},{"full_name":"Güntert, Peter","first_name":"Peter","last_name":"Güntert"},{"full_name":"Favier, Adrien","first_name":"Adrien","last_name":"Favier"},{"full_name":"Schoehn, Guy","last_name":"Schoehn","first_name":"Guy"},{"first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"last_name":"Boisbouvier","first_name":"Jerome","full_name":"Boisbouvier, Jerome"}],"article_number":"2697","extern":"1"},{"article_type":"original","publication":"Science Advances","citation":{"chicago":"Felix, Jan, Katharina Weinhäupl, Christophe Chipot, François Dehez, Audrey Hessel, Diego F. Gauto, Cecile Morlot, et al. “Mechanism of the Allosteric Activation of the ClpP Protease Machinery by Substrates and Active-Site Inhibitors.” Science Advances. American Association for the Advancement of Science, 2019. https://doi.org/10.1126/sciadv.aaw3818.","mla":"Felix, Jan, et al. “Mechanism of the Allosteric Activation of the ClpP Protease Machinery by Substrates and Active-Site Inhibitors.” Science Advances, vol. 5, no. 9, eaaw3818, American Association for the Advancement of Science, 2019, doi:10.1126/sciadv.aaw3818.","short":"J. Felix, K. Weinhäupl, C. Chipot, F. Dehez, A. Hessel, D.F. Gauto, C. Morlot, O. Abian, I. Gutsche, A. Velazquez-Campoy, P. Schanda, H. Fraga, Science Advances 5 (2019).","ista":"Felix J, Weinhäupl K, Chipot C, Dehez F, Hessel A, Gauto DF, Morlot C, Abian O, Gutsche I, Velazquez-Campoy A, Schanda P, Fraga H. 2019. Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors. Science Advances. 5(9), eaaw3818.","ieee":"J. Felix et al., “Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors,” Science Advances, vol. 5, no. 9. American Association for the Advancement of Science, 2019.","apa":"Felix, J., Weinhäupl, K., Chipot, C., Dehez, F., Hessel, A., Gauto, D. F., … Fraga, H. (2019). Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors. Science Advances. American Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aaw3818","ama":"Felix J, Weinhäupl K, Chipot C, et al. Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors. Science Advances. 2019;5(9). doi:10.1126/sciadv.aaw3818"},"date_published":"2019-09-04T00:00:00Z","day":"04","article_processing_charge":"No","status":"public","title":"Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors","intvolume":" 5","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"8406","oa_version":"Published Version","type":"journal_article","abstract":[{"lang":"eng","text":"Coordinated conformational transitions in oligomeric enzymatic complexes modulate function in response to substrates and play a crucial role in enzyme inhibition and activation. Caseinolytic protease (ClpP) is a tetradecameric complex, which has emerged as a drug target against multiple pathogenic bacteria. Activation of different ClpPs by inhibitors has been independently reported from drug development efforts, but no rationale for inhibitor-induced activation has been hitherto proposed. Using an integrated approach that includes x-ray crystallography, solid- and solution-state nuclear magnetic resonance, molecular dynamics simulations, and isothermal titration calorimetry, we show that the proteasome inhibitor bortezomib binds to the ClpP active-site serine, mimicking a peptide substrate, and induces a concerted allosteric activation of the complex. The bortezomib-activated conformation also exhibits a higher affinity for its cognate unfoldase ClpX. We propose a universal allosteric mechanism, where substrate binding to a single subunit locks ClpP into an active conformation optimized for chaperone association and protein processive degradation."}],"issue":"9","quality_controlled":"1","oa":1,"main_file_link":[{"open_access":"1","url":" https://doi.org/10.1126/sciadv.aaw3818"}],"language":[{"iso":"eng"}],"doi":"10.1126/sciadv.aaw3818","month":"09","publication_identifier":{"issn":["2375-2548"]},"publication_status":"published","publisher":"American Association for the Advancement of Science","year":"2019","date_created":"2020-09-17T10:28:36Z","date_updated":"2021-01-12T08:19:03Z","volume":5,"author":[{"full_name":"Felix, Jan","last_name":"Felix","first_name":"Jan"},{"first_name":"Katharina","last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina"},{"full_name":"Chipot, Christophe","first_name":"Christophe","last_name":"Chipot"},{"last_name":"Dehez","first_name":"François","full_name":"Dehez, François"},{"full_name":"Hessel, Audrey","last_name":"Hessel","first_name":"Audrey"},{"full_name":"Gauto, Diego F.","first_name":"Diego F.","last_name":"Gauto"},{"first_name":"Cecile","last_name":"Morlot","full_name":"Morlot, Cecile"},{"full_name":"Abian, Olga","last_name":"Abian","first_name":"Olga"},{"last_name":"Gutsche","first_name":"Irina","full_name":"Gutsche, Irina"},{"last_name":"Velazquez-Campoy","first_name":"Adrian","full_name":"Velazquez-Campoy, Adrian"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul"},{"full_name":"Fraga, Hugo","last_name":"Fraga","first_name":"Hugo"}],"article_number":"eaaw3818","extern":"1"},{"volume":141,"date_created":"2020-09-17T10:29:50Z","date_updated":"2021-01-12T08:19:07Z","author":[{"full_name":"Rovó, Petra","last_name":"Rovó","first_name":"Petra"},{"full_name":"Smith, Colin A.","first_name":"Colin A.","last_name":"Smith"},{"full_name":"Gauto, Diego","last_name":"Gauto","first_name":"Diego"},{"first_name":"Bert L.","last_name":"de Groot","full_name":"de Groot, Bert L."},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul"},{"first_name":"Rasmus","last_name":"Linser","full_name":"Linser, Rasmus"}],"publisher":"American Chemical Society","publication_status":"published","pmid":1,"year":"2019","extern":"1","language":[{"iso":"eng"}],"doi":"10.1021/jacs.8b09258","quality_controlled":"1","external_id":{"pmid":["30620186"]},"publication_identifier":{"issn":["0002-7863","1520-5126"]},"month":"01","oa_version":"Submitted Version","intvolume":" 141","title":"Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"8413","issue":"2","abstract":[{"lang":"eng","text":"NMR relaxation dispersion methods provide a holistic way to observe microsecond time-scale protein backbone motion both in solution and in the solid state. Different nuclei (1H and 15N) and different relaxation dispersion techniques (Bloch–McConnell and near-rotary-resonance) give complementary information about the amplitudes and time scales of the conformational dynamics and provide comprehensive insights into the mechanistic details of the structural rearrangements. In this paper, we exemplify the benefits of the combination of various solution- and solid-state relaxation dispersion methods on a microcrystalline protein (α-spectrin SH3 domain), for which we are able to identify and model the functionally relevant conformational rearrangements around the ligand recognition loop occurring on multiple microsecond time scales. The observed loop motions suggest that the SH3 domain exists in a binding-competent conformation in dynamic equilibrium with a sterically impaired ground-state conformation both in solution and in crystalline form. This inherent plasticity between the interconverting macrostates is compatible with a conformational-preselection model and provides new insights into the recognition mechanisms of SH3 domains."}],"type":"journal_article","date_published":"2019-01-08T00:00:00Z","page":"858-869","article_type":"original","citation":{"chicago":"Rovó, Petra, Colin A. Smith, Diego Gauto, Bert L. de Groot, Paul Schanda, and Rasmus Linser. “Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.” Journal of the American Chemical Society. American Chemical Society, 2019. https://doi.org/10.1021/jacs.8b09258.","mla":"Rovó, Petra, et al. “Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques.” Journal of the American Chemical Society, vol. 141, no. 2, American Chemical Society, 2019, pp. 858–69, doi:10.1021/jacs.8b09258.","short":"P. Rovó, C.A. Smith, D. Gauto, B.L. de Groot, P. Schanda, R. Linser, Journal of the American Chemical Society 141 (2019) 858–869.","ista":"Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. 2019. Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. 141(2), 858–869.","ieee":"P. Rovó, C. A. Smith, D. Gauto, B. L. de Groot, P. Schanda, and R. Linser, “Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques,” Journal of the American Chemical Society, vol. 141, no. 2. American Chemical Society, pp. 858–869, 2019.","apa":"Rovó, P., Smith, C. A., Gauto, D., de Groot, B. L., Schanda, P., & Linser, R. (2019). Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. American Chemical Society. https://doi.org/10.1021/jacs.8b09258","ama":"Rovó P, Smith CA, Gauto D, de Groot BL, Schanda P, Linser R. Mechanistic insights into microsecond time-scale motion of solid proteins using complementary 15N and 1H relaxation dispersion techniques. Journal of the American Chemical Society. 2019;141(2):858-869. doi:10.1021/jacs.8b09258"},"publication":"Journal of the American Chemical Society","article_processing_charge":"No","day":"08","keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"]},{"citation":{"ieee":"M. D. Shannon et al., “Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR,” ChemPhysChem, vol. 20, no. 2. Wiley, pp. 311–317, 2019.","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. ChemPhysChem. Wiley. https://doi.org/10.1002/cphc.201800779","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.","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. ChemPhysChem. 2019;20(2):311-317. doi:10.1002/cphc.201800779","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.” ChemPhysChem. Wiley, 2019. https://doi.org/10.1002/cphc.201800779.","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.","mla":"Shannon, Matthew D., et al. “Conformational Dynamics in the Core of Human Y145Stop Prion Protein Amyloid Probed by Relaxation Dispersion NMR.” ChemPhysChem, vol. 20, no. 2, Wiley, 2019, pp. 311–17, doi:10.1002/cphc.201800779."},"publication":"ChemPhysChem","page":"311-317","article_type":"original","date_published":"2019-01-21T00:00:00Z","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"article_processing_charge":"No","day":"21","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"8412","intvolume":" 20","status":"public","title":"Conformational dynamics in the core of human Y145Stop prion protein amyloid probed by relaxation dispersion NMR","oa_version":"Submitted Version","type":"journal_article","issue":"2","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."}],"external_id":{"pmid":["30276945"]},"quality_controlled":"1","doi":"10.1002/cphc.201800779","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1439-4235"]},"month":"01","pmid":1,"year":"2019","publisher":"Wiley","publication_status":"published","author":[{"first_name":"Matthew D.","last_name":"Shannon","full_name":"Shannon, Matthew D."},{"first_name":"Theint","last_name":"Theint","full_name":"Theint, Theint"},{"full_name":"Mukhopadhyay, Dwaipayan","last_name":"Mukhopadhyay","first_name":"Dwaipayan"},{"last_name":"Surewicz","first_name":"Krystyna","full_name":"Surewicz, Krystyna"},{"full_name":"Surewicz, Witold K.","first_name":"Witold K.","last_name":"Surewicz"},{"full_name":"Marion, Dominique","last_name":"Marion","first_name":"Dominique"},{"last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul"},{"last_name":"Jaroniec","first_name":"Christopher P.","full_name":"Jaroniec, Christopher P."}],"volume":20,"date_created":"2020-09-17T10:29:43Z","date_updated":"2021-01-12T08:19:06Z","extern":"1"},{"year":"2019","pmid":1,"publication_status":"published","publisher":"Wiley","author":[{"full_name":"Marion, Dominique","first_name":"Dominique","last_name":"Marion"},{"first_name":"Diego F.","last_name":"Gauto","full_name":"Gauto, Diego F."},{"first_name":"Isabel","last_name":"Ayala","full_name":"Ayala, Isabel"},{"full_name":"Giandoreggio-Barranco, Karine","last_name":"Giandoreggio-Barranco","first_name":"Karine"},{"first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"}],"date_updated":"2021-01-12T08:19:06Z","date_created":"2020-09-17T10:29:36Z","volume":20,"extern":"1","external_id":{"pmid":["30444575"]},"quality_controlled":"1","doi":"10.1002/cphc.201800935","language":[{"iso":"eng"}],"month":"01","publication_identifier":{"issn":["1439-4235"]},"_id":"8411","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","title":"Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR","intvolume":" 20","oa_version":"Submitted Version","type":"journal_article","abstract":[{"lang":"eng","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."}],"issue":"2","publication":"ChemPhysChem","citation":{"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.","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,” ChemPhysChem, vol. 20, no. 2. Wiley, pp. 276–284, 2019.","apa":"Marion, D., Gauto, D. F., 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. Wiley. https://doi.org/10.1002/cphc.201800935","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. ChemPhysChem. 2019;20(2):276-284. doi:10.1002/cphc.201800935","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.” ChemPhysChem. Wiley, 2019. https://doi.org/10.1002/cphc.201800935.","mla":"Marion, Dominique, et al. “Microsecond Protein Dynamics from Combined Bloch-McConnell and Near-Rotary-Resonance R1p Relaxation-Dispersion MAS NMR.” ChemPhysChem, vol. 20, no. 2, Wiley, 2019, pp. 276–84, doi:10.1002/cphc.201800935.","short":"D. Marion, D.F. Gauto, I. Ayala, K. Giandoreggio-Barranco, P. Schanda, ChemPhysChem 20 (2019) 276–284."},"article_type":"original","page":"276-284","date_published":"2019-01-21T00:00:00Z","keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"day":"21","article_processing_charge":"No"}]