{"year":"2019","intvolume":"        20","volume":20,"keyword":["Physical and Theoretical Chemistry","Atomic and Molecular Physics","and Optics"],"external_id":{"pmid":["30444575"]},"publication_identifier":{"issn":["1439-4235"]},"author":[{"full_name":"Marion, Dominique","last_name":"Marion","first_name":"Dominique"},{"full_name":"Gauto, Diego F.","last_name":"Gauto","first_name":"Diego F."},{"first_name":"Isabel","last_name":"Ayala","full_name":"Ayala, Isabel"},{"last_name":"Giandoreggio-Barranco","first_name":"Karine","full_name":"Giandoreggio-Barranco, Karine"},{"orcid":"0000-0002-9350-7606","first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul"}],"publication":"ChemPhysChem","doi":"10.1002/cphc.201800935","page":"276-284","_id":"8411","language":[{"iso":"eng"}],"article_type":"original","citation":{"short":"D. Marion, D.F. Gauto, I. Ayala, K. Giandoreggio-Barranco, P. Schanda, ChemPhysChem 20 (2019) 276–284.","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>","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>.","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.","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>","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.","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>."},"publisher":"Wiley","oa_version":"Submitted Version","date_created":"2020-09-17T10:29:36Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","quality_controlled":"1","title":"Microsecond protein dynamics from combined Bloch-McConnell and Near-Rotary-Resonance R1p relaxation-dispersion MAS NMR","status":"public","article_processing_charge":"No","month":"01","pmid":1,"date_updated":"2021-01-12T08:19:06Z","type":"journal_article","day":"21","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."}],"date_published":"2019-01-21T00:00:00Z","extern":"1","publication_status":"published","issue":"2"}