Structural similarity of a membrane protein in micelles and membranes. J Am Chem Soc 2007 Jul 04;129(26):8078-9
Date
06/15/2007Pubmed ID
17567018Pubmed Central ID
PMC2518691DOI
10.1021/ja0728371Scopus ID
2-s2.0-34447135010 (requires institutional sign-in at Scopus site) 47 CitationsAbstract
The anisotropic spin interactions measured for membrane proteins in weakly oriented micelles and in oriented lipid bilayers provide independent and potentially complementary high-resolution restraints for structure determination. Here we show that the membrane protein CHIF adopts a similar structure in lipid micelles and bilayers, allowing the restraints from micelle and bilayer samples to be combined in a complementary fashion to enhance the structural information. Back-calculation and assignment of the NMR spectrum of CHIF in oriented lipid bilayers, from the structure determined in micelles, provides additional restraints for structure determination as well as the global orientation of the protein in the membrane. The combined use of solution and solid-state NMR restraints also affords cross-validation for the structural analysis.
Author List
Franzin CM, Teriete P, Marassi FMAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Cell MembraneMembrane Proteins
Micelles
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
