Identification of protein folds: matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures |
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| Authors: | J U Bowie N D Clarke C O Pabo R T Sauer |
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| Affiliation: | Department of Biology, Massachusetts Institute of Technology, Cambridge 02139. |
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| Abstract: | Hydrophobic side chains often are buried in the interior of a protein, and evolutionarily related proteins usually maintain the hydrophobic character of buried positions. In this paper we show that a pattern of hydrophobicity values derived from a set of related protein sequences is well correlated with the linear pattern of side-chain solvent accessibility values, calculated from a known protein structure representative of the sequences. In several cases, information from aligned sequences can be used to select the correct tertiary fold from a large data base of protein structures. |
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