Similar energetic contributions of packing in the core of membrane and water-soluble proteins.
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ABSTRACT:
SUBMITTER: Joh NH
PROVIDER: S-EPMC2744480 | biostudies-literature | 2009 Aug
REPOSITORIES: biostudies-literature
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Similar energetic contributions of packing in the core of membrane and water-soluble proteins.
Joh Nathan H NH Oberai Amit A Yang Duan D Whitelegge Julian P JP Bowie James U JU
Journal of the American Chemical Society 20090801 31
A major driving force for water-soluble protein folding is the hydrophobic effect, but membrane proteins cannot make use of this stabilizing contribution in the apolar core of the bilayer. It has been proposed that membrane proteins compensate by packing more efficiently. We therefore investigated packing contributions experimentally by observing the energetic and structural consequences of cavity creating mutations in the core of a membrane protein. We observed little difference in the packing ...[more]
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