Modulating membrane protein stability and association by design.
Membrane proteins perform crucial communication functions across biological membranes. They represent important targets for therapies and have unique properties for biotechnological applications. Recently, the number of high-resolution membrane protein structures has significantly increased and new insights into the sequence/structure relationships of transmembrane helical assemblies have been gained. Together with new experimental techniques, these advances have improved our understanding of membrane protein folding, stability, and recognition. Consequently, new design strategies are emerging that aim to target and stabilize simple transmembrane helical interfaces.
Barth
Patrick
P
Department of Biochemistry, University of Washington, Seattle, WA 98195, USA. barthp@u.washington.edu
D000818:Animals; D019295:Computational Biology; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D015202:Protein Engineering / Q000379:methods / Q000639:trends; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D008565:Membrane Proteins