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Local sequence patterns of hydrophobicity and solvent accessibility in soluble globular proteins
Author(s) -
Lipman David J.,
Pastor Richard W.,
Lee B.
Publication year - 1987
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360260106
Subject(s) - chemistry , sequence (biology) , globular protein , globular cluster , solvent , peptide sequence , amino acid , protein evolution , crystallography , biochemistry , physics , quantum mechanics , galaxy , gene
We examined the variation in the solvent accessibility and hydrophobicity of the amino acids along the sequences of 58 soluble globular proteins with known tertiary structure. We found that there is a significant tendency for the accessibilities to run in clusters along the sequence but that the hydrophobicities are distributed without such nonrandom clusters. Theseresults suggest severe limitations on the power of sequence analysis tools that use average hydrophobicity scores of overlapping subsequences to predict accessibility.