--- res: bibo_abstract: - '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.@eng' bibo_authorlist: - foaf_Person: foaf_givenName: Diego F. foaf_name: Gauto, Diego F. foaf_surname: Gauto - foaf_Person: foaf_givenName: Audrey foaf_name: Hessel, Audrey foaf_surname: Hessel - foaf_Person: foaf_givenName: Petra foaf_name: Rovó, Petra foaf_surname: Rovó - foaf_Person: foaf_givenName: Vilius foaf_name: Kurauskas, Vilius foaf_surname: Kurauskas - foaf_Person: foaf_givenName: Rasmus foaf_name: Linser, Rasmus foaf_surname: Linser - foaf_Person: foaf_givenName: Paul foaf_name: Schanda, Paul foaf_surname: Schanda foaf_workInfoHomepage: http://www.librecat.org/personId=7B541462-FAF6-11E9-A490-E8DFE5697425 orcid: 0000-0002-9350-7606 bibo_doi: 10.1016/j.ssnmr.2017.04.002 bibo_issue: '10' bibo_volume: 87 dct_date: 2017^xs_gYear dct_isPartOf: - http://id.crossref.org/issn/0926-2040 dct_language: eng dct_publisher: Elsevier@ dct_subject: - Nuclear and High Energy Physics - Instrumentation - General Chemistry - Radiation dct_title: 'Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals@' ...