Structure determination of membrane proteins by NMR spectroscopy. Biochem Cell Biol 2002;80(5):597-604
Date
11/21/2002Pubmed ID
12440700Pubmed Central ID
PMC3454473DOI
10.1139/o02-154Scopus ID
2-s2.0-0036968507 (requires institutional sign-in at Scopus site) 59 CitationsAbstract
Current strategies for determining the structures of membrane proteins in lipid environments by NMR spectroscopy rely on the anisotropy of nuclear spin interactions, which are experimentally accessible through experiments performed on weakly and completely aligned samples. Importantly, the anisotropy of nuclear spin interactions results in a mapping of structure to the resonance frequencies and splittings observed in NMR spectra. Distinctive wheel-like patterns are observed in two-dimensional 1H-15N heteronuclear dipolar/15N chemical shift PISEMA (polarization inversion spin-exchange at the magic angle) spectra of helical membrane proteins in highly aligned lipid bilayer samples. One-dimensional dipolar waves are an extension of two-dimensional PISA (polarity index slant angle) wheels that map protein structures in NMR spectra of both weakly and completely aligned samples. Dipolar waves describe the periodic wave-like variations of the magnitudes of the heteronuclear dipolar couplings as a function of residue number in the absence of chemical shift effects. Since weakly aligned samples of proteins display these same effects, primarily as residual dipolar couplings, in solution NMR spectra, this represents a convergence of solid-state and solution NMR approaches to structure determination.
Author List
Opella SJ, Nevzorov A, Mesleh MF, 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
AnimalsChemical Phenomena
Chemistry, Physical
Crystallization
Humans
Hydrogen Bonding
Lipid Bilayers
Membrane Proteins
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
