Toward optimal-resolution NMR of intrinsically disordered
proteins

J 2014

Toward optimal-resolution NMR of intrinsically disordered proteins

NOVÁČEK, Jiří, Lukáš ŽÍDEK a Vladimír SKLENÁŘ

Základní údaje

Originální název

Toward optimal-resolution NMR of intrinsically disordered proteins

Autoři

NOVÁČEK, Jiří (203 Česká republika, domácí), Lukáš ŽÍDEK (203 Česká republika, domácí) a Vladimír SKLENÁŘ (203 Česká republika, garant, domácí)

Vydání

Journal of Magnetic Resonance, San Diego, Academic Press Inc Elsevier Science, 2014, 1090-7807

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.510

Kód RIV

RIV/00216224:14740/14:00073570

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.jmr.2013.12.008

UT WoS

000334653600005

Klíčová slova anglicky

IDPs; IDPRs; Multi-dimensional NMR; Non-uniform sampling; NUS; PRE; RDC; RNAP delta-subunit

Štítky

kontrola MP, ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 17. 10. 2014 13:45, Martina Prášilová

Anotace

V originále

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.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GAP206/11/0758, projekt VaV

Název: Vývoj metodologie s vysokým rozlišením pro NMR studie neuspořádaných proteinů s vysoce degenerovanými rezonančními frekvencemi (Akronym: HIGHRES)

Investor: Grantová agentura ČR, Vývoj metodologie s vysokým rozlišením pro NMR studie neuspořádaných proteinů s vysoce degenerovanými rezonančními frekvencemi

261863, interní kód MU

Název: BioNMR Facilities - Bio NMR (Akronym: BioNMR)

Investor: Evropská unie, BioNMR Facilities - Bio NMR, Kapacity

Citovat

NOVÁČEK, Jiří, Lukáš ŽÍDEK a Vladimír SKLENÁŘ. Toward optimal-resolution NMR of intrinsically disordered proteins. Journal of Magnetic Resonance. San Diego: Academic Press Inc Elsevier Science, 2014, roč. 241, April, s. 41-52. ISSN 1090-7807. Dostupné z: https://dx.doi.org/10.1016/j.jmr.2013.12.008.

@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 a Vladimír SKLENÁŘ. Toward optimal-resolution NMR of intrinsically disordered proteins. \textit{Journal of Magnetic Resonance}. San Diego: Academic Press Inc Elsevier Science, 2014, roč.~241, April, s.~41-52. ISSN~1090-7807. Dostupné z: https://dx.doi.org/10.1016/j.jmr.2013.12.008.

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