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Perturbed interaction between residues 85 and 204 in Tyr-185-->Phe and Asp-85-->Glu bacteriorhodopsins.

According to earlier reports, residue 85 in the bacteriorhodopsin mutants D85E and Y185F deprotonates with two apparent pKa values. Additionally, in Y185F, Asp-85 becomes significantly more protonated during light adaptation. We provide a new explanation for these findings. It is based on the scheme...

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Detalhes bibliográficos
Main Authors: Richter, H T, Needleman, R, Lanyi, J K
Formato: Artigo
Idioma:Inglês
Publicado em: 1996
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC1233826/
https://ncbi.nlm.nih.gov/pubmed/8968608
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