Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Am Chem Soc. 2009 Aug 12;131(31):10846-7. doi: 10.1021/ja904711k.

Similar energetic contributions of packing in the core of membrane and water-soluble proteins.

Author information

  • 1Department of Chemistry and Biochemistry, UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles, California 90095, USA.

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.

PMID:
19603754
[PubMed - indexed for MEDLINE]
PMCID:
PMC2744480
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for American Chemical Society Icon for PubMed Central
    Loading ...
    Write to the Help Desk