Similar energetic contributions of packing in the core of membrane and water-soluble proteins.
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.
Joh
Nathan H
NH
Department of Chemistry and Biochemistry, UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles, California 90095, USA.
Oberai
Amit
A
Yang
Duan
D
Whitelegge
Julian P
JP
Bowie
James U
JU
D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000737:chemistry*; D008956:Models, Chemical; D009154:Mutation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012995:Solubility
D008565:Membrane Proteins; D011506:Proteins