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Published online before print November 22, 2006, 10.1110/ps.062383807
Protein Science (2007), 16:125-134. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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FOR THE RECORD

BPPred: A Web-based computational tool for predicting biophysical parameters of proteins

Christian D. Geierhaas1,2, Adrian A. Nickson1,2, Kresten Lindorff-Larsen2, Jane Clarke1,2, and Michele Vendruscolo2

1 MRC Centre for Protein Engineering, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom
2 Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom

(RECEIVED June 5, 2006; FINAL REVISION September 17, 2006; ACCEPTED September 18, 2006)

We exploit the availability of recent experimental data on a variety of proteins to develop a Web-based prediction algorithm (BPPred) to calculate several biophysical parameters commonly used to describe the folding process. These parameters include the equilibrium m-values, the length of proteins, and the changes upon unfolding in the solvent-accessible surface area, in the heat capacity, and in the radius of gyration. We also show that the knowledge of any one of these quantities allows an estimate of the others to be obtained, and describe the confidence limits with which these estimations can be made. Furthermore, we discuss how the kinetic m-values, or the Beta Tanford values, may provide an estimate of the solvent-accessible surface area and the radius of gyration of the transition state for protein folding. Taken together, these results suggest that BPPred should represent a valuable tool for interpreting experimental measurements, as well as the results of molecular dynamics simulations.

Keywords: protein denaturation; urea; guanidine hydrochloride; guanidinium chloride; protein folding; m-values; SASA; radius of gyration; heat capacity; transition state; unfolded state; denatured state


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C. D. Geierhaas, X. Salvatella, J. Clarke, and M. Vendruscolo
Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values
Protein Eng. Des. Sel., March 1, 2008; 21(3): 215 - 222.
[Abstract] [Full Text] [PDF]


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