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Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation

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Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation. / Paquin, Raphaël; Ferrage, Fabien; Mulder, Frans A A et al.

In: Journal of the American Chemical Society, Vol. 130, No. 47, 26.11.2008, p. 15805-15807.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Paquin, R, Ferrage, F, Mulder, FAA, Akke, M & Bodenhausen, G 2008, 'Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation', Journal of the American Chemical Society, vol. 130, no. 47, pp. 15805-15807. https://doi.org/10.1021/ja803794g

APA

Paquin, R., Ferrage, F., Mulder, F. A. A., Akke, M., & Bodenhausen, G. (2008). Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation. Journal of the American Chemical Society, 130(47), 15805-15807. https://doi.org/10.1021/ja803794g

CBE

Paquin R, Ferrage F, Mulder FAA, Akke M, Bodenhausen G. 2008. Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation. Journal of the American Chemical Society. 130(47):15805-15807. https://doi.org/10.1021/ja803794g

MLA

Vancouver

Paquin R, Ferrage F, Mulder FAA, Akke M, Bodenhausen G. Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation. Journal of the American Chemical Society. 2008 Nov 26;130(47):15805-15807. https://doi.org/10.1021/ja803794g

Author

Paquin, Raphaël ; Ferrage, Fabien ; Mulder, Frans A A et al. / Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation. In: Journal of the American Chemical Society. 2008 ; Vol. 130, No. 47. pp. 15805-15807.

Bibtex

@article{773c64031c684548b8babe2a38f9515a,
title = "Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation",
abstract = "Side-chain carboxyl and carbonyl groups play a major role in protein interactions and enzyme catalysis. A series of 13C relaxation experiments is introduced to study the dynamics of carboxyl and carbonyl groups in protein side chains on both fast (sub-ns) and slower (μs-ms) time scales. This approach is illustrated on the protein calbindin D9k. Fast dynamics features correlate with hydrogen- and ion-binding patterns. We also identify chemical dynamics on μs time scales in solvent-exposed carboxyl groups, most probably due to exchange between the carboxylate and carboxylic acid forms.",
author = "Rapha{\"e}l Paquin and Fabien Ferrage and Mulder, {Frans A A} and Mikael Akke and Geoffrey Bodenhausen",
year = "2008",
month = nov,
day = "26",
doi = "10.1021/ja803794g",
language = "English",
volume = "130",
pages = "15805--15807",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "47",

}

RIS

TY - JOUR

T1 - Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation

AU - Paquin, Raphaël

AU - Ferrage, Fabien

AU - Mulder, Frans A A

AU - Akke, Mikael

AU - Bodenhausen, Geoffrey

PY - 2008/11/26

Y1 - 2008/11/26

N2 - Side-chain carboxyl and carbonyl groups play a major role in protein interactions and enzyme catalysis. A series of 13C relaxation experiments is introduced to study the dynamics of carboxyl and carbonyl groups in protein side chains on both fast (sub-ns) and slower (μs-ms) time scales. This approach is illustrated on the protein calbindin D9k. Fast dynamics features correlate with hydrogen- and ion-binding patterns. We also identify chemical dynamics on μs time scales in solvent-exposed carboxyl groups, most probably due to exchange between the carboxylate and carboxylic acid forms.

AB - Side-chain carboxyl and carbonyl groups play a major role in protein interactions and enzyme catalysis. A series of 13C relaxation experiments is introduced to study the dynamics of carboxyl and carbonyl groups in protein side chains on both fast (sub-ns) and slower (μs-ms) time scales. This approach is illustrated on the protein calbindin D9k. Fast dynamics features correlate with hydrogen- and ion-binding patterns. We also identify chemical dynamics on μs time scales in solvent-exposed carboxyl groups, most probably due to exchange between the carboxylate and carboxylic acid forms.

U2 - 10.1021/ja803794g

DO - 10.1021/ja803794g

M3 - Journal article

C2 - 18975903

AN - SCOPUS:56749180963

VL - 130

SP - 15805

EP - 15807

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 47

ER -