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• W1519243724 abstract "The EF‐hand calcium‐binding proteins may exist either in an extended or a compact conformation. This conformation is sometimes correlated with the function of the calcium‐binding protein. For those proteins whose structure and function are known, calcium sensors are usually extended and calcium buffers compact; hence, there is interest in predicting the form of the protein starting from its sequence. In the present study, we used two different procedures: one that already exists in the literature, the sosuidumbbell algorithm, mainly based on the charges of the two EF‐hand domains, and the other comprising a novel procedure that is based on linker average hydrophilicity. The linker consists of the residues that connect the domains. The two procedures were tested on 17 known‐structure calcium‐binding proteins and then applied to 59 unknown‐structure centrins. The sosuidumbbell algorithm yielded the correct conformations for only 15 of the known‐structure proteins and predicted that all centrins should be in a closed form. The linker average hydrophilicity procedure discriminated well between all the extended and non‐extended forms of the known‐structure calcium‐binding proteins, and its prediction concerning centrins reflected well their phylogenetic classification. The linker average hydrophilicity criterion is a simple and powerful means to discriminate between extended and non‐extended forms of calcium‐binding proteins. What is remarkable is that only a few residues that constitute the linker (between 2 and 20 in our tested sample of proteins) are responsible for the form of the calcium‐binding protein, showing that this form is mainly governed by short‐range interactions." @default.
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• W1519243724 date "2009-01-23" @default.
• W1519243724 modified "2023-10-18" @default.
• W1519243724 title "What determines the degree of compactness of a calcium-binding protein?" @default.
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• W1519243724 doi "https://doi.org/10.1111/j.1742-4658.2008.06851.x" @default.
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