Residue-specific millisecond to microsecond fluctuations in bacteriorhodopsin induced by disrupted or disorganized two-dimensional crystalline lattice, through modified lipid–helix and helix–helix interactions, as revealed by 13C NMR
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference63 articles.
1. Intramembrane Helix-Helix Association in Oligomerization and Transmembrane Signaling
2. Structure and Stability of Membrane Proteins
3. Electron-crystallographic Refinement of the Structure of Bacteriorhodopsin
4. X-ray Structure of Bacteriorhodopsin at 2.5 Angstroms from Microcrystals Grown in Lipidic Cubic Phases
5. Proton Transfer Pathways in Bacteriorhodopsin at 2.3 Angstrom Resolution
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1. Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer;Journal of the American Chemical Society;2022-02-14
2. Identification of Specific Effect of Chloride on the Spectral Properties and Structural Stability of Multiple Extracellular Glutamic Acid Mutants of Bacteriorhodopsin;PLOS ONE;2016-09-22
3. Dynamic Pictures of Proteins by NMR;Annual Reports on NMR Spectroscopy;2014
4. Electrostatic effects influence the formation of two-dimensional crystals of bacteriorhodopsin reconstituted into dimyristoylphosphatidylcholine membranes;Journal of Biochemistry;2011-04-09
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