Solid-state NMR investigation of the buried X-proline peptide bonds of bacteriorhodopsin |
| |
Authors: | Lansing Jonathan C Hu Jingui G Belenky Marina Griffin Robert G Herzfeld Judith |
| |
Institution: | Department of Chemistry and Center for Magnetic Resonance, Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139-4307, USA. |
| |
Abstract: | The role of proline residues in the photocycle of bacteriorhodopsin (bR) is addressed using solid-state NMR. (13)C and (15)N chemical shifts from X-Pro peptide bonds in bR are assigned from REDOR difference spectra of pairwise labeled samples, and correlations of chemical shifts with structure are explored in a series of X-Pro model compounds. Results for the three membrane-embedded X-Pro bonds of bR indicate only slight changes in the transition from the resting state of the protein to either the early or late M state of the protonmotive photocycle. These results suggest that the buried prolines serve a principally structural role in bR. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|