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@article{1173973, author = {Nováček, Jiří and Žídek, Lukáš and Sklenář, Vladimír}, article_location = {San Diego}, article_number = {April}, doi = {http://dx.doi.org/10.1016/j.jmr.2013.12.008}, keywords = {IDPs; IDPRs; Multi-dimensional NMR; Non-uniform sampling; NUS; PRE; RDC; RNAP delta-subunit}, language = {eng}, issn = {1090-7807}, journal = {Journal of Magnetic Resonance}, title = {Toward optimal-resolution NMR of intrinsically disordered proteins}, url = {http://dx.doi.org/10.1016/j.jmr.2013.12.008}, volume = {241}, year = {2014} }
TY - JOUR ID - 1173973 AU - Nováček, Jiří - Žídek, Lukáš - Sklenář, Vladimír PY - 2014 TI - Toward optimal-resolution NMR of intrinsically disordered proteins JF - Journal of Magnetic Resonance VL - 241 IS - April SP - 41-52 EP - 41-52 PB - Academic Press Inc Elsevier Science SN - 10907807 KW - IDPs KW - IDPRs KW - Multi-dimensional NMR KW - Non-uniform sampling KW - NUS KW - PRE KW - RDC KW - RNAP delta-subunit UR - http://dx.doi.org/10.1016/j.jmr.2013.12.008 L2 - http://dx.doi.org/10.1016/j.jmr.2013.12.008 N2 - 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. ER -
NOVÁČEK, Jiří, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. Toward optimal-resolution NMR of intrinsically disordered proteins. \textit{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.
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