4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective
HCBCANCO experiments for the sequential assignment and chemical
shift analysis of intrinsically disordered proteins

J 2012

4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins

NOVÁČEK, Jiří, Noam Y HABA, Jordan H CHILL, Lukáš ŽÍDEK, Vladimír SKLENÁŘ et. al.

Základní údaje

Originální název

4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins

Autoři

NOVÁČEK, Jiří (203 Česká republika, domácí), Noam Y HABA (376 Izrael), Jordan H CHILL (376 Izrael), Lukáš ŽÍDEK (203 Česká republika, garant, domácí) a Vladimír SKLENÁŘ (203 Česká republika, domácí)

Vydání

Journal of Biomolecular NMR, Dordrecht, Springer Netherlands, 2012, 0925-2738

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10610 Biophysics

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.845

Kód RIV

RIV/00216224:14740/12:00057624

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1007/s10858-012-9631-8

UT WoS

000305943400007

Klíčová slova anglicky

Intrinsically disordered proteins; Non-uniform sampling; C-13 detection; Chemical shifts; Residual secondary structure; Prolines assignment

Štítky

ok, rivok

Změněno: 7. 5. 2013 06:52, prof. Mgr. Lukáš Žídek, Ph.D.

Anotace

V originále

A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit C-13 direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (H-alpha, and H-beta) and carbon (C-alpha, C-beta) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient secondary structure motifs in the intrinsically disordered proteins (H-alpha, C-alpha, C-beta, C', and N) can be extracted from each spectrum. Compared to the commonly used assignment strategy based on matching the C-alpha and C-beta chemical shifts, inclusion of the H-alpha and H-beta provides up to three extra resonance frequencies that decrease the chance of ambiguous assignment. The experiments were successfully applied to the original assignment of a 12.8 kDa intrinsically disordered protein having a high content of proline residues (26 %) in the sequence.

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

228461, interní kód MU

Název: Enhancing Access and Services to East European users Towards an efficient (Akronym: EAST-NMR)

Investor: Evropská unie, Enhancing Access and Services to East European users Towards an efficient, Kapacity

Citovat

NOVÁČEK, Jiří, Noam Y HABA, Jordan H CHILL, Lukáš ŽÍDEK a Vladimír SKLENÁŘ. 4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins. Journal of Biomolecular NMR. Dordrecht: Springer Netherlands, 2012, roč. 53, č. 2, s. 139-148. ISSN 0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-012-9631-8.

@article{1066896,
   author = {Nováček, Jiří and Haba, Noam Y and Chill, Jordan H and Žídek, Lukáš and Sklenář, Vladimír},
   article_location = {Dordrecht},
   article_number = {2},
   doi = {http://dx.doi.org/10.1007/s10858-012-9631-8},
   keywords = {Intrinsically disordered proteins; Non-uniform sampling; C-13 detection; Chemical shifts; Residual secondary structure; Prolines assignment},
   language = {eng},
   issn = {0925-2738},
   journal = {Journal of Biomolecular NMR},
   title = {4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins},
   url = {http://www.springerlink.com/content/g5116115mh441831/?MUD=MP},
   volume = {53},
   year = {2012}
}

TY  - JOUR
ID  - 1066896
AU  - Nováček, Jiří - Haba, Noam Y - Chill, Jordan H - Žídek, Lukáš - Sklenář, Vladimír
PY  - 2012
TI  - 4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
JF  - Journal of Biomolecular NMR
VL  - 53
IS  - 2
SP  - 139-148
EP  - 139-148
PB  - Springer Netherlands
SN  - 09252738
KW  - Intrinsically disordered proteins
KW  - Non-uniform sampling
KW  - C-13 detection
KW  - Chemical shifts
KW  - Residual secondary structure
KW  - Prolines assignment
UR  - http://www.springerlink.com/content/g5116115mh441831/?MUD=MP
L2  - http://www.springerlink.com/content/g5116115mh441831/?MUD=MP
N2  - A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit C-13 direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (H-alpha, and H-beta) and carbon (C-alpha, C-beta) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient secondary structure motifs in the intrinsically disordered proteins (H-alpha, C-alpha, C-beta, C', and N) can be extracted from each spectrum. Compared to the commonly used assignment strategy based on matching the C-alpha and C-beta chemical shifts, inclusion of the H-alpha and H-beta provides up to three extra resonance frequencies that decrease the chance of ambiguous assignment. The experiments were successfully applied to the original assignment of a 12.8 kDa intrinsically disordered protein having a high content of proline residues (26 %) in the sequence.
ER  -

NOVÁČEK, Jiří, Noam Y HABA, Jordan H CHILL, Lukáš ŽÍDEK a Vladimír SKLENÁŘ. 4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins. \textit{Journal of Biomolecular NMR}. Dordrecht: Springer Netherlands, 2012, roč.~53, č.~2, s.~139-148. ISSN~0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-012-9631-8.

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