Determination of helix-helix interactions in membranes by rotational resonance NMR.
Determination of helix-helix interactions in membranes by rotational resonance NMR.
http://www.ncbi.nlm.nih.gov/corehtml...pubmed-pmc.gif Related Articles Determination of helix-helix interactions in membranes by rotational resonance NMR. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):488-91 Authors: Smith SO, Bormann BJ Dimerization of human glycophorin A in erythrocyte membranes is mediated by specific interactions within the helical transmembrane domain of the protein. Rotational resonance NMR provides a unique approach for obtaining high-resolution structural data in membrane systems and has been used to establish intermolecular contacts in the glycophorin A dimer by using hydrophobic peptides that correspond to the transmembrane sequence. Magnetization exchange rates were measured between [13C]methyl labels in the hydrophobic sequence -G79-V80-M81-A82-G83-V84- located in the middle of the transmembrane domain and specific [13C]carbonyl labels along the peptide backbone across the dimer interface. Significant magnetization exchange was observed only between V80 (13CH3) and G79 (13C = O) and between V84 (13CH3) and G83 (13C = O), indicating that these residues are packed in the dimer interface in a "ridges-ingrooves" arrangement. PMID: 7831316 [PubMed - indexed for MEDLINE] Source: PubMed |
All times are GMT. The time now is 10:09 AM. |
Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Search Engine Friendly URLs by vBSEO 3.6.0
Copyright, BioNMR.com, 2003-2013