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Local sequence patterns of hydrophobicity and solvent accessibility in soluble globular proteins

✍ Scribed by David J. Lipman; Richard W. Pastor; B. Lee

Publisher: Wiley (John Wiley & Sons)
Year: 1987
Tongue: English
Weight: 510 KB
Volume: 26
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360260106

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✦ Synopsis

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 ionrandom clusters. These results suggest severe limitations on the power of sequence analysis tools that use average hydrophobicity scores of overlapping subsequences to predict accessibility.

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