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Cited by 161

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Determination of an Ensemble of Structures Representing the Denatured State of the Bovine Acyl-Coenzyme A Binding Protein

Lindorff-Larsen, Kresten, Kristjansdottir, Sigridur, Teilum, Kaare, Fieber, Wolfgang, Dobson, Christopher M., Poulsen, Flemming M., Vendruscolo, Michele·2004·Journal of the American Chemical Society
DOI 10.1021/ja039250g
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Abstract

The denatured state of a protein contains important information about the determinants of the folding process. By combining site-directed spin-labeling NMR experiments and restrained computer simulations, we have determined ensembles of conformations that represent the denatured state of the bovine acyl-coenzyme A binding protein (ACBP) at three different concentrations of guanidine hydrochloride. As the experimentally determined distance information corresponds to weighted averages over a broad ensemble of structures, we applied the experimental restraints to a system of noninteracting replicas of the protein by using a Monte Carlo sampling scheme. This procedure permits us to sample ensembles of conformations that are compatible with the experimental data and thus to obtain information regarding the distribution of structures in the denatured state. Our results show that the denatured state of ACBP is highly heterogeneous. The high sensitivity of the computational method that we present, however, enabled us to identify long-range interactions between two regions, located near the N- and C-termini, that include both native and non-native elements. The preferential formation of these contacts suggests that the sequence-dependent patterns of helical propensity and hydrophobicity are important determinants of the structure in the denatured state of ACBP.

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Cited by

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Metadata

Authors
Lindorff-Larsen, K., Kristjansdottir, S., Teilum, K., Fieber, W., Dobson, C. M., Poulsen, F. M., & Vendruscolo, M.
Venue
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Published
2004-02-20
Volume
126
Issue
10
Pages
3291-3299
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
DOI
10.1021/ja039250g
OpenAlex
W2074586183
Cited by
161
References
3
FWCI
4.26
Type
journal article
Language
en
Open access
closed

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