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Slow cooperative folding of a small globular protein HPr.
Biochemistry. 1998 Jan 13; 37(2):622-37.B

Abstract

The folding of an 85-residue protein, the histidine-containing phosphocarrier protein HPr, has been studied using a variety of techniques including DSC, CD, ANS fluorescence, and NMR spectroscopy. In both kinetic and equilibrium experiments the unfolding of HPr can be adequately described as a two-state process which does not involve the accumulation of intermediates. Thermodynamic characterization of the native and the transition states has been achieved from both equilibrium and kinetic experiments. The heat capacity change from the denatured state to the transition state (3. 2 kJ mol-1 K-1) is half of the heat capacity difference between the native and denatured states (6.3 kJ mol-1 K-1), while the solvent accessibility of the transition state (0.36) indicates that its compactness is closer to that of the native than that of the denatured state. The high value for the change in heat capacity upon unfolding results in the observation of cold denaturation at moderate denaturant concentrations. Refolding from high denaturant concentrations is, however, slow. The rate constant of folding in water, (14.9 s-1), is small compared to that reported for other proteins of similar size under similar conditions. This indicates that very fast refolding is not a universal character of small globular proteins which fold in the absence of detectable intermediates.

Authors+Show Affiliations

New Chemistry Laboratory, Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford OX1 3QT, U.K.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9425085

Citation

Van Nuland, N A., et al. "Slow Cooperative Folding of a Small Globular Protein HPr." Biochemistry, vol. 37, no. 2, 1998, pp. 622-37.
Van Nuland NA, Meijberg W, Warner J, et al. Slow cooperative folding of a small globular protein HPr. Biochemistry. 1998;37(2):622-37.
Van Nuland, N. A., Meijberg, W., Warner, J., Forge, V., Scheek, R. M., Robillard, G. T., & Dobson, C. M. (1998). Slow cooperative folding of a small globular protein HPr. Biochemistry, 37(2), 622-37.
Van Nuland NA, et al. Slow Cooperative Folding of a Small Globular Protein HPr. Biochemistry. 1998 Jan 13;37(2):622-37. PubMed PMID: 9425085.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Slow cooperative folding of a small globular protein HPr. AU - Van Nuland,N A, AU - Meijberg,W, AU - Warner,J, AU - Forge,V, AU - Scheek,R M, AU - Robillard,G T, AU - Dobson,C M, PY - 1998/2/21/pubmed PY - 1998/2/21/medline PY - 1998/2/21/entrez SP - 622 EP - 37 JF - Biochemistry JO - Biochemistry VL - 37 IS - 2 N2 - The folding of an 85-residue protein, the histidine-containing phosphocarrier protein HPr, has been studied using a variety of techniques including DSC, CD, ANS fluorescence, and NMR spectroscopy. In both kinetic and equilibrium experiments the unfolding of HPr can be adequately described as a two-state process which does not involve the accumulation of intermediates. Thermodynamic characterization of the native and the transition states has been achieved from both equilibrium and kinetic experiments. The heat capacity change from the denatured state to the transition state (3. 2 kJ mol-1 K-1) is half of the heat capacity difference between the native and denatured states (6.3 kJ mol-1 K-1), while the solvent accessibility of the transition state (0.36) indicates that its compactness is closer to that of the native than that of the denatured state. The high value for the change in heat capacity upon unfolding results in the observation of cold denaturation at moderate denaturant concentrations. Refolding from high denaturant concentrations is, however, slow. The rate constant of folding in water, (14.9 s-1), is small compared to that reported for other proteins of similar size under similar conditions. This indicates that very fast refolding is not a universal character of small globular proteins which fold in the absence of detectable intermediates. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/9425085/Slow_cooperative_folding_of_a_small_globular_protein_HPr_ L2 - https://doi.org/10.1021/bi9717946 DB - PRIME DP - Unbound Medicine ER -