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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.