Opening the Schiff base moiety of bacteriorhodopsin by mutation of the four extracellular Glu side chains
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sameAs
Identification of Specific Effect of Chloride on the Spectral Properties and Structural Stability of Multiple Extracellular Glutamic Acid Mutants of Bacteriorhodopsin.Contribution of extracellular Glu residues to the structure and function of bacteriorhodopsin. Presence of specific cation-binding sites.Thr90 is a key residue of the bacteriorhodopsin proton pumping mechanism.Thr-90 plays a vital role in the structure and function of bacteriorhodopsin.pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin.
P2860
Opening the Schiff base moiety of bacteriorhodopsin by mutation of the four extracellular Glu side chains
description
im Juli 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published on 01 July 1999
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в липні 1999
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name
Opening the Schiff base moiety ...... extracellular Glu side chains
@en
Opening the Schiff base moiety ...... extracellular Glu side chains
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type
label
Opening the Schiff base moiety ...... extracellular Glu side chains
@en
Opening the Schiff base moiety ...... extracellular Glu side chains
@nl
prefLabel
Opening the Schiff base moiety ...... extracellular Glu side chains
@en
Opening the Schiff base moiety ...... extracellular Glu side chains
@nl
P2093
P2860
P921
P1433
P1476
Opening the Schiff base moiety ...... extracellular Glu side chains
@en
P2093
J L Bourdelande
R González-Moreno
T Lazarova
P2860
P304
P356
10.1016/S0014-5793(99)00950-3
P407
P577
1999-07-01T00:00:00Z