pH-induced structural changes in bacteriorhodopsin studied by Fourier transform infrared spectroscopy.

Previous C13-NMR studies showed that two of the four internal aspartic acid residues (Asp-96 and Asp-115) of bacteriorhodopsin (bR) are protonated up to pH = 10, but no accurate pKa of these residues has been determined. In this work, infrared spectroscopy with the attenuated total reflection techni...

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Main Authors: Száraz, S, Oesterhelt, D, Ormos, P
Format: Artigo
Jezik:Inglês
Izdano: 1994
Teme:
Research Article
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC1225532/
https://ncbi.nlm.nih.gov/pubmed/7819502
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