| Literature DB >> 19603754 |
Nathan H Joh1, Amit Oberai, Duan Yang, Julian P Whitelegge, James U Bowie.
Abstract
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 energetics of water and membrane soluble proteins. Our results imply that other mechanisms are employed to stabilize the structure of membrane proteins.Entities:
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Year: 2009 PMID： 19603754 PMCID： PMC2744480 DOI： 10.1021/ja904711k
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419