ArticleProtein science : a publication of the Protein Society2007
BPPred: a Web-based computational tool for predicting biophysical parameters of proteins.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 61 citations in OpenAlex.
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- Effect of BET Missense Mutations on Bromodomain Function, Inhibitor Binding and Stability.PloS one · 2016Article
- Understanding the effect of alternative splicing in the folding and function of the second PDZ from protein tyrosine phosphatase-BL.Scientific reports · 2015Article
- Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- High thermodynamic stability of parametrically designed helical bundles.Science (New York, N.Y.) · 2014Article
- Random single amino acid deletion sampling unveils structural tolerance and the benefits of helical registry shift on GFP folding and structure.Structure (London, England : 1993) · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
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.
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