NOVÁČEK, Jiří, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. Toward optimal-resolution NMR of intrinsically disordered proteins. Journal of Magnetic Resonance. San Diego: Academic Press Inc Elsevier Science, 2014, vol. 241, April, p. 41-52. ISSN 1090-7807. Available from: https://dx.doi.org/10.1016/j.jmr.2013.12.008.
Other formats:   BibTeX LaTeX RIS
Basic information
Original name Toward optimal-resolution NMR of intrinsically disordered proteins
Authors NOVÁČEK, Jiří (203 Czech Republic, belonging to the institution), Lukáš ŽÍDEK (203 Czech Republic, belonging to the institution) and Vladimír SKLENÁŘ (203 Czech Republic, guarantor, belonging to the institution).
Edition Journal of Magnetic Resonance, San Diego, Academic Press Inc Elsevier Science, 2014, 1090-7807.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 2.510
RIV identification code RIV/00216224:14740/14:00073570
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1016/j.jmr.2013.12.008
UT WoS 000334653600005
Keywords in English IDPs; IDPRs; Multi-dimensional NMR; Non-uniform sampling; NUS; PRE; RDC; RNAP delta-subunit
Tags kontrola MP, ok, rivok
Tags International impact, Reviewed
Changed by Changed by: Martina Prášilová, učo 342282. Changed: 17/10/2014 13:45.
Abstract
Proteins, which, in their native conditions, sample a multitude of distinct conformational states characterized by high spatiotemporal heterogeneity, most often termed as intrinsically disordered proteins (IDPs), have become a target of broad interest over the past 15 years. With the growing evidence of their important roles in fundamental cellular processes, there is an urgent need to characterize the conformational behavior of IDPs at the highest possible level. The unique feature of NMR spectroscopy in the context of IDPs is its ability to supply details of their structural and temporal alterations at atomic-level resolution. Here, we briefly review recently proposed NMR-based strategies to characterize transient states populated by IDPs and summarize the latest achievements and future prospects in methodological development. Because low chemical shift dispersion represents the major obstacle encountered when studying IDPs by nuclear magnetic resonance, particular attention is paid to techniques allowing one to approach the physical limits of attainable resolution.
Links
ED1.1.00/02.0068, research and development projectName: CEITEC - central european institute of technology
GAP206/11/0758, research and development projectName: Vývoj metodologie s vysokým rozlišením pro NMR studie neuspořádaných proteinů s vysoce degenerovanými rezonančními frekvencemi (Acronym: HIGHRES)
Investor: Czech Science Foundation
261863, interní kód MUName: BioNMR Facilities - Bio NMR (Acronym: BioNMR)
Investor: European Union, Capacities
PrintDisplayed: 25/4/2024 12:27