Identification of protein folds: Matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures | Zendy

Bowie James U. | Zendy; Clarke Neil D. | Zendy; Pabo Carl O. | Zendy; Sauer Robert T. | Zendy

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Identification of protein folds: Matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures

Author(s) -

Bowie James U.,

Clarke Neil D.,

Pabo Carl O.,

Sauer Robert T.

Publication year - 1990

Publication title -

proteins: structure, function, and bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.699

H-Index - 191

eISSN - 1097-0134

pISSN - 0887-3585

DOI - 10.1002/prot.340070307

Subject(s) - sequence (biology) , side chain , identification (biology) , set (abstract data type) , protein tertiary structure , protein structure , matching (statistics) , solvent , biological system , chemistry , crystallography , computational biology , computer science , pattern recognition (psychology) , biology , artificial intelligence , biochemistry , mathematics , polymer , organic chemistry , statistics , botany , programming language

Hydrophobic side chains often are buried in the interior of a protein, and evolutionarily related proteins usually maintain the hydrophobic character of buried position. In this paper we shown 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 database of protein structures.

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