{"citation":{"ista":"Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. 2017. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. 87(10), 86–95.","chicago":"Gauto, Diego F., Audrey Hessel, Petra Rovó, Vilius Kurauskas, Rasmus Linser, and Paul Schanda. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” <i>Solid State Nuclear Magnetic Resonance</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>.","apa":"Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., &#38; Schanda, P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. <i>Solid State Nuclear Magnetic Resonance</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>","ama":"Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. <i>Solid State Nuclear Magnetic Resonance</i>. 2017;87(10):86-95. doi:<a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">10.1016/j.ssnmr.2017.04.002</a>","mla":"Gauto, Diego F., et al. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” <i>Solid State Nuclear Magnetic Resonance</i>, vol. 87, no. 10, Elsevier, 2017, pp. 86–95, doi:<a href=\"https://doi.org/10.1016/j.ssnmr.2017.04.002\">10.1016/j.ssnmr.2017.04.002</a>.","short":"D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid State Nuclear Magnetic Resonance 87 (2017) 86–95.","ieee":"D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda, “Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals,” <i>Solid State Nuclear Magnetic Resonance</i>, vol. 87, no. 10. Elsevier, pp. 86–95, 2017."},"month":"10","date_created":"2020-09-18T10:06:18Z","keyword":["Nuclear and High Energy Physics","Instrumentation","General Chemistry","Radiation"],"article_processing_charge":"No","date_published":"2017-10-01T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","year":"2017","publisher":"Elsevier","article_type":"original","page":"86-95","day":"01","publication_identifier":{"issn":["0926-2040"]},"intvolume":"        87","language":[{"iso":"eng"}],"date_updated":"2021-01-12T08:19:20Z","volume":87,"extern":"1","type":"journal_article","publication_status":"published","issue":"10","publication":"Solid State Nuclear Magnetic Resonance","oa_version":"None","abstract":[{"lang":"eng","text":"Solid-state NMR spectroscopy can provide site-resolved information about protein dynamics over many time scales. Here we combine protein deuteration, fast magic-angle spinning (~45–60 kHz) and proton detection to study dynamics of ubiquitin in microcrystals, and in particular a mutant in a region that undergoes microsecond motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation dispersion, to probe how the G53A mutation alters these dynamics. We report a population-inversion of conformational states: the conformation that in the wild-type protein is populated only sparsely becomes the predominant state. We furthermore explore the potential to use amide-1H R1ρ relaxation to obtain insight into dynamics. We show that while quantitative interpretation of 1H relaxation remains beyond reach under the experimental conditions, due to coherent contributions to decay, one may extract qualitative information about flexibility."}],"_id":"8447","author":[{"full_name":"Gauto, Diego F.","first_name":"Diego F.","last_name":"Gauto"},{"last_name":"Hessel","first_name":"Audrey","full_name":"Hessel, Audrey"},{"first_name":"Petra","full_name":"Rovó, Petra","last_name":"Rovó"},{"last_name":"Kurauskas","first_name":"Vilius","full_name":"Kurauskas, Vilius"},{"last_name":"Linser","first_name":"Rasmus","full_name":"Linser, Rasmus"},{"orcid":"0000-0002-9350-7606","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda"}],"doi":"10.1016/j.ssnmr.2017.04.002","quality_controlled":"1","title":"Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals"}