Toward optimal-resolution NMR of intrinsically disordered proteins

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00073570" target="_blank" >RIV/00216224:14740/14:00073570 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.jmr.2013.12.008" target="_blank" >http://dx.doi.org/10.1016/j.jmr.2013.12.008</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jmr.2013.12.008" target="_blank" >10.1016/j.jmr.2013.12.008</a>

Result language
angličtina
Original language name
Toward optimal-resolution NMR of intrinsically disordered proteins
Original language description
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 spectroscopyin 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.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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