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PubMed · 1366953

Repacking protein interiors.

W S Sandberg·T C Terwilliger
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Abstract

Several goals of protein engineering may be achieved through redesign and repacking of protein interiors. The effects of interior apolar substitutions on protein stability depend strongly on the site of the substitution. One reason for this is that protein interiors have properties both of apolar liquids and of crystalline solids. Substitutions at interior sites affect the stability of a protein by changing the hydrophobicity, but each site in a protein has a characteristic energy associated with introducing packing changes, and the net stability depends on both of these factors.

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Models, ChemicalProtein ConformationProtein EngineeringStructure-Activity RelationshipThermodynamicsJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.Review

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W S Sandberg, T C Terwilliger. 1991. Repacking protein interiors.. https://doi.org/10.1016/0167-7799(91)90190-s

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