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Microsecond protein dynamics measured by C-13(alpha) rotating-frame spin relaxation

Lundström, Patrik LU and Akke, Mikael LU (2005) In ChemBioChem 6(9). p.1685-1692
Abstract
NMR spin relaxation in the rotating frame (R-1p) is a unique method for atomic-resolution characterisation of conformational (chemical) exchange processes occuring on the microsecond timescale. We present a rotating frame C-13 relaxation dispersion experiment for measuring conformational dynamics in uniformly C-13-labeled proteins. The experiment was validated by using the E140Q mutant of the C-terminal fragment of calmodulin, which exhibits significant conformational exchange between two major conformations, as gauged from previous N-15 and H-1 relaxation studies. Consistent with previous work, the present C-13, R-1p experiment detects conformational-exchange dynamics throughout the protein. The average correlation time of <tau(ex)>... (More)
NMR spin relaxation in the rotating frame (R-1p) is a unique method for atomic-resolution characterisation of conformational (chemical) exchange processes occuring on the microsecond timescale. We present a rotating frame C-13 relaxation dispersion experiment for measuring conformational dynamics in uniformly C-13-labeled proteins. The experiment was validated by using the E140Q mutant of the C-terminal fragment of calmodulin, which exhibits significant conformational exchange between two major conformations, as gauged from previous N-15 and H-1 relaxation studies. Consistent with previous work, the present C-13, R-1p experiment detects conformational-exchange dynamics throughout the protein. The average correlation time of <tau(ex)> = 25 +/- 8 mu s is in excellent agreement with those determined previously from H-1 and N-15 R-1p, relaxation data: <tau(ex)> = 19 +/- 7 and 21 +/- 3 mu s, respectively. The extracted chemical-shift differences between the exchanging states reveal significant fluctuations in dihedral angles within single regions of Ramachandran phi-psi space that were not identified from the H-1 and N-15 relaxation data. The present results underscore the advantage of using several types of nuclei to probe exchange dynamics in biomolecules. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
ChemBioChem
volume
6
issue
9
pages
1685 - 1692
publisher
John Wiley & Sons
external identifiers
  • wos:000231769700022
  • pmid:16028301
  • scopus:24744459108
ISSN
1439-4227
DOI
10.1002/cbic.200500086
language
English
LU publication?
yes
id
23aa7dda-f3c4-44ab-afa0-f4cb282b02c9 (old id 151500)
date added to LUP
2007-06-29 13:18:08
date last changed
2017-02-26 03:38:17
@article{23aa7dda-f3c4-44ab-afa0-f4cb282b02c9,
  abstract     = {NMR spin relaxation in the rotating frame (R-1p) is a unique method for atomic-resolution characterisation of conformational (chemical) exchange processes occuring on the microsecond timescale. We present a rotating frame C-13 relaxation dispersion experiment for measuring conformational dynamics in uniformly C-13-labeled proteins. The experiment was validated by using the E140Q mutant of the C-terminal fragment of calmodulin, which exhibits significant conformational exchange between two major conformations, as gauged from previous N-15 and H-1 relaxation studies. Consistent with previous work, the present C-13, R-1p experiment detects conformational-exchange dynamics throughout the protein. The average correlation time of &lt;tau(ex)&gt; = 25 +/- 8 mu s is in excellent agreement with those determined previously from H-1 and N-15 R-1p, relaxation data: &lt;tau(ex)&gt; = 19 +/- 7 and 21 +/- 3 mu s, respectively. The extracted chemical-shift differences between the exchanging states reveal significant fluctuations in dihedral angles within single regions of Ramachandran phi-psi space that were not identified from the H-1 and N-15 relaxation data. The present results underscore the advantage of using several types of nuclei to probe exchange dynamics in biomolecules.},
  author       = {Lundström, Patrik and Akke, Mikael},
  issn         = {1439-4227},
  language     = {eng},
  number       = {9},
  pages        = {1685--1692},
  publisher    = {John Wiley & Sons},
  series       = {ChemBioChem},
  title        = {Microsecond protein dynamics measured by C-13(alpha) rotating-frame spin relaxation},
  url          = {http://dx.doi.org/10.1002/cbic.200500086},
  volume       = {6},
  year         = {2005},
}