Solid-state NMR investigation of the buried X-proline peptide bonds of bacteriorhodop
 

Solid-state NMR investigation of the buried X-proline peptide bonds of bacteriorhodopsin.

Related Articles Solid-state NMR investigation of the buried X-proline peptide bonds of bacteriorhodopsin.

Biochemistry. 2003 Apr 1;42(12):3586-93

Authors: Lansing JC, Hu JG, Belenky M, Griffin RG, Herzfeld J

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.

PMID: 12653563 [PubMed - indexed for MEDLINE]



Source: PubMed