Literature DB >> 17870471

Modulating membrane protein stability and association by design.

Patrick Barth1.   

Abstract

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.

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Year:  2007        PMID: 17870471     DOI: 10.1016/j.sbi.2007.08.006

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  2 in total

1.  Residue-specific side-chain packing determines the backbone dynamics of transmembrane model helices.

Authors:  Stefan Quint; Simon Widmaier; David Minde; Daniel Hornburg; Dieter Langosch; Christina Scharnagl
Journal:  Biophys J       Date:  2010-10-20       Impact factor: 4.033

2.  Naturally evolved G protein-coupled receptors adopt metastable conformations.

Authors:  Kuang-Yui Michael Chen; Fuguo Zhou; Bartlomiej G Fryszczyn; Patrick Barth
Journal:  Proc Natl Acad Sci U S A       Date:  2012-07-30       Impact factor: 11.205

  2 in total

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