Asp96 deprotonation and transmembrane alpha-helical structural changes in bacteriorhodopsin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference50 articles.
1. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
2. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
3. Fourier Transform Infrared Techniques for Probing Membrane Protein Structure
4. Role of aspartate-96 in proton translocation by bacteriorhodopsin.
5. Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence for the interaction of aspartic acid 212 with tyrosine 185 and possible role in the proton pump mechanism.
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