Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Similar energetic contributions of packing in the core of membrane and water-soluble proteins.,Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU. Similar energetic contributions of packing in the core of membrane and water-soluble proteins. J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754 doi:10.1021/ja904711k
