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

Raphaël Paquin; Fabien Ferrage; Frans A A Mulder; Mikael Akke; Geoffrey Bodenhausen

doi:10.1021/ja803794g

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

Raphaël Paquin, Fabien Ferrage^*, Frans A A Mulder, Mikael Akke, Geoffrey Bodenhausen

^*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

36 Citations (Scopus)

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 D_9k. 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.

Original language	English
Journal	Journal of the American Chemical Society
Volume	130
Issue	47
Pages (from-to)	15805-15807
Number of pages	3
ISSN	0002-7863
DOIs	https://doi.org/10.1021/ja803794g
Publication status	Published - 26 Nov 2008
Externally published	Yes

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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",

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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 newspaper › Journal article › Research › peer-review

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

SN - 0002-7863

VL - 130

SP - 15805

EP - 15807

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 47

ER -

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

Abstract

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