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• W2099779674 startingPage "387" @default.
• W2099779674 abstract "Various studies suggest that the hydrophobic effect plays a major role in driving the folding of proteins. In the past, however, it has been challenging to translate this understanding into a predictive, quantitative theory of how the full pattern of sequence hydrophobicity in a protein shapes functionally important features of its tertiary structure. Here, we extend and apply such a phenomenological theory of the sequence-structure relationship in globular protein domains, which had previously been applied to the study of allosteric motion. In an effort to optimize parameters for the model, we first analyze the patterns of backbone burial found in single-domain crystal structures, and discover that classic hydrophobicity scales derived from bulk physicochemical properties of amino acids are already nearly optimal for prediction of burial using the model. Subsequently, we apply the model to studying structural fluctuations in proteins and establish a means of identifying ligand-binding and protein–protein interaction sites using this approach." @default.
• W2099779674 created "2016-06-24" @default.
• W2099779674 creator A5007425055 @default.
• W2099779674 creator A5022792589 @default.
• W2099779674 date "2014-02-19" @default.
• W2099779674 modified "2023-09-27" @default.
• W2099779674 title "Quantitative theory of hydrophobic effect as a driving force of protein structure" @default.
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• W2099779674 doi "https://doi.org/10.1002/pro.2420" @default.
• W2099779674 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3970890" @default.
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• W2099779674 hasPublicationYear "2014" @default.
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