Literature DB >> 18975903

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

Raphaël Paquin1, Fabien Ferrage, Frans A A Mulder, Mikael Akke, Geoffrey Bodenhausen.   

Abstract

Side-chain carboxyl and carbonyl groups play a major role in protein interactions and enzyme catalysis. A series of (13)C relaxation experiments is introduced to study the dynamics of carboxyl and carbonyl groups in protein side chains on both fast (sub-ns) and slower (micros-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 micros time scales in solvent-exposed carboxyl groups, most probably due to exchange between the carboxylate and carboxylic acid forms.

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Year:  2008        PMID： 18975903     DOI： 10.1021/ja803794g

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


  19 in total

1.  Nuclear overhauser spectroscopy of chiral CHD methylene groups.

Authors:  Rafal Augustyniak; Jan Stanek; Henri Colaux; Geoffrey Bodenhausen; Wiktor Koźmiński; Torsten Herrmann; Fabien Ferrage
Journal:  J Biomol NMR       Date:  2015-11-27       Impact factor: 2.835

2.  Protein conformational exchange measured by 1H R1ρ relaxation dispersion of methyl groups.

Authors:  Ulrich Weininger; Annica T Blissing; Janosch Hennig; Alexandra Ahlner; Zhihong Liu; Hans J Vogel; Mikael Akke; Patrik Lundström
Journal:  J Biomol NMR       Date:  2013-08-02       Impact factor: 2.835

3.  Solution structure and backbone dynamics of the DNA-binding domain of FOXP1: insight into its domain swapping and DNA binding.

Authors:  Yuan-Ping Chu; Chia-Hao Chang; Jia-Hau Shiu; Yao-Tsung Chang; Chiu-Yueh Chen; Woei-Jer Chuang
Journal:  Protein Sci       Date:  2011-04-11       Impact factor: 6.725

4.  Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R(1ρ): an application to αB-crystallin.

Authors:  Andrew J Baldwin; Lewis E Kay
Journal:  J Biomol NMR       Date:  2012-04-05       Impact factor: 2.835

5.  Comprehensive determination of protein tyrosine pKa values for photoactive yellow protein using indirect 13C NMR spectroscopy.

Authors:  Nur Alia Oktaviani; Trijntje J Pool; Hironari Kamikubo; Jelle Slager; Ruud M Scheek; Mikio Kataoka; Frans A A Mulder
Journal:  Biophys J       Date:  2012-02-07       Impact factor: 4.033

6.  Side chain dynamics of carboxyl and carbonyl groups in the catalytic function of Escherichia coli ribonuclease H.

Authors:  Kate A Stafford; Fabien Ferrage; Jae-Hyun Cho; Arthur G Palmer
Journal:  J Am Chem Soc       Date:  2013-11-20       Impact factor: 15.419

7.  Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r).

Authors:  Renee Otten; Janice Villali; Dorothee Kern; Frans A A Mulder
Journal:  J Am Chem Soc       Date:  2010-11-08       Impact factor: 15.419

8.  Protein side-chain dynamics and residual conformational entropy.

Authors:  Nikola Trbovic; Jae-Hyun Cho; Robert Abel; Richard A Friesner; Mark Rance; Arthur G Palmer
Journal:  J Am Chem Soc       Date:  2009-01-21       Impact factor: 15.419

9.  Conformational entropy changes upon lactose binding to the carbohydrate recognition domain of galectin-3.

Authors:  Carl Diehl; Samuel Genheden; Kristofer Modig; Ulf Ryde; Mikael Akke
Journal:  J Biomol NMR       Date:  2009-07-30       Impact factor: 2.835

10.  Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected ¹³C CPMG relaxation dispersion.

Authors:  Ulrich Weininger; Michal Respondek; Mikael Akke
Journal:  J Biomol NMR       Date:  2012-07-26       Impact factor: 2.835
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