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- Title
Conformational heterogeneity of transmembrane residues after the Schiff base reprotonation of bacteriorhodopsin.
- Authors
Mason, A. James; Turner, George J.; Glaubitz, Clemens
- Abstract
bR, N-like and O-like intermediate states of[15N]methionine-labelled wild type and D85N/T170C bacteriorhodopsin were accumulated in native membranes by controlling the pH of the preparations.15N cross polarization and magic angle sample spinning (CPMAS) NMR spectroscopy allowed resolution of seven out of nine resonances in the bR-state. It was possible to assign some of the observed resonances by using13C/15N rotational echo double resonance (REDOR) NMR and Mn2+ quenchingas well as D2O exchange, which helps to identify conformational changes after the bacteriorhodopsin Schiff base reprotonation. The significant differences in chemical shifts and linewidths detected for some of the resonances in N- and O-like samples indicate changes in conformation, structural heterogeneity or altered molecular dynamics in parts of the protein.
- Subjects
BACTERIORHODOPSIN; BACTERIAL pigments; BACTERIAL proteins; HALOBACTERIUM; PROTEINS; BIOMOLECULES; BIOLOGICAL membranes
- Publication
FEBS Journal, 2005, Vol 272, Issue 9, p2152
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2005.04633.x