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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...

詳細記述

保存先:
書誌詳細
主要な著者: Richter, H T, Needleman, R, Lanyi, J K
フォーマット: Artigo
言語:Inglês
出版事項: 1996
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC1233826/
https://ncbi.nlm.nih.gov/pubmed/8968608
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