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.

Basic information

Original name

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

Authors

NOVÁČEK, Jiří (203 Czech Republic, belonging to the institution), Noam Y HABA (376 Israel), Jordan H CHILL (376 Israel), Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution) and Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution)

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10610 Biophysics

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 2.845

RIV identification code

RIV/00216224:14740/12:00057624

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000305943400007

Keywords in English

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

Abstract

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.

Links

ED1.1.00/02.0068, research and development project

Name: CEITEC - central european institute of technology

GAP206/11/0758, research and development project

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

Investor: Czech Science Foundation

228461, interní kód MU

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

Investor: European Union, Enhancing Access and Services to East European users Towards an efficient, Capacities

Citovat

NOVÁČEK, Jiří, Noam Y HABA, Jordan H CHILL, Lukáš ŽÍDEK and 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, vol. 53, No 2, p. 139-148. ISSN 0925-2738. Available from: 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 and 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, vol.~53, No~2, p.~139-148. ISSN~0925-2738. Available from: https://dx.doi.org/10.1007/s10858-012-9631-8.

Detailed Information on Publication Record