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Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP

Modig, Kristofer LU and Poulsen, Flemming M. (2008) In Journal of Biomolecular NMR 42(3). p.163-177
Abstract
We have investigated the acid-unfolded state of acyl-coenzyme A binding protein (ACBP) using N-15 laboratory frame nuclear magnetic resonance (NMR) relaxation experiments at three magnetic field strengths. The data have been analyzed using standard model-free fitting and models involving distribution of correlation times. In particular, a model-independent method of analysis that does not assume any analytical form for the correlation time distribution is proposed. This method explains correlations between model-free parameters and the analytical distribution parameters found by other authors. The analysis also shows that the relaxation data are consistent with and complementary to information obtained from other parameters, especially... (More)
We have investigated the acid-unfolded state of acyl-coenzyme A binding protein (ACBP) using N-15 laboratory frame nuclear magnetic resonance (NMR) relaxation experiments at three magnetic field strengths. The data have been analyzed using standard model-free fitting and models involving distribution of correlation times. In particular, a model-independent method of analysis that does not assume any analytical form for the correlation time distribution is proposed. This method explains correlations between model-free parameters and the analytical distribution parameters found by other authors. The analysis also shows that the relaxation data are consistent with and complementary to information obtained from other parameters, especially secondary chemical shifts and residual dipolar couplings, and strengthens the conclusions of previous observations that three out of the four regions that form helices in the native structure appear to contain residual secondary structure also in the acid-denatured state. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Model-free, Relaxation, NMR, Acid-denaturation, ACBP, Protein folding
in
Journal of Biomolecular NMR
volume
42
issue
3
pages
163 - 177
publisher
Springer
external identifiers
  • wos:000260281800003
  • scopus:55649093500
ISSN
1573-5001
DOI
10.1007/s10858-008-9280-0
language
English
LU publication?
yes
id
c3a988b8-9921-4904-89b1-1daf4cf682ee (old id 1284651)
date added to LUP
2009-02-09 09:53:20
date last changed
2017-11-12 03:23:59
@article{c3a988b8-9921-4904-89b1-1daf4cf682ee,
  abstract     = {We have investigated the acid-unfolded state of acyl-coenzyme A binding protein (ACBP) using N-15 laboratory frame nuclear magnetic resonance (NMR) relaxation experiments at three magnetic field strengths. The data have been analyzed using standard model-free fitting and models involving distribution of correlation times. In particular, a model-independent method of analysis that does not assume any analytical form for the correlation time distribution is proposed. This method explains correlations between model-free parameters and the analytical distribution parameters found by other authors. The analysis also shows that the relaxation data are consistent with and complementary to information obtained from other parameters, especially secondary chemical shifts and residual dipolar couplings, and strengthens the conclusions of previous observations that three out of the four regions that form helices in the native structure appear to contain residual secondary structure also in the acid-denatured state.},
  author       = {Modig, Kristofer and Poulsen, Flemming M.},
  issn         = {1573-5001},
  keyword      = {Model-free,Relaxation,NMR,Acid-denaturation,ACBP,Protein folding},
  language     = {eng},
  number       = {3},
  pages        = {163--177},
  publisher    = {Springer},
  series       = {Journal of Biomolecular NMR},
  title        = {Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP},
  url          = {http://dx.doi.org/10.1007/s10858-008-9280-0},
  volume       = {42},
  year         = {2008},
}