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Exploiting lipid interactions to control membrane protein insertion, folding and stability
Author(s) -
Booth Paula
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a423-e
Subject(s) - bilayer , lipid bilayer , transmembrane protein , membrane protein , membrane curvature , chemistry , biophysics , membrane , protein folding , elasticity of cell membranes , peripheral membrane protein , folding (dsp implementation) , curvature , crystallography , biochemistry , integral membrane protein , lipid bilayer phase behavior , biology , receptor , engineering , electrical engineering , geometry , mathematics
Efficient systems need to be developed to unfold and re‐fold alpha helical membrane proteins. We have been developing in vitro lipid‐bilayer folding systems for membrane proteins. The stored curvature elastic stress of model bilayers can be used to optimise the rate and yield of folded protein. We have shown that events such as transmembrane helix insertion, as well as tertiary and quaternary structure formation are altered by the stored curvature stress of the bilayer. The curvature stress of a phosphatoidylcholine lipid bilayer can be altered by changing either the lipid chains or introducing a different headgroup such as phosphoethanolamine. We have developed the approach on a halobacterial protein and since applied it to other membrane proteins.