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Updated: Aug 9, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
From structure to mechanism: electron crystallographic studies of bacteriorhodopsin
Sriram Subramaniam1, Teruhisa Hirai, Richard Henderson
1Laboratory of Biochemistry, National Cancer Institute, National Instititutes of Health, Bethesda, MD 20817, USA.
Abstract:
Bacteriorhodopsin is a protein found in cell membranes of the organism H. salinarum, where it functions as an efficient light-driven proton pump. Because bacteriorhodopsin is one of the simplest ion pumps known in biology, it has been the subject of intensive investigations over the last three decades, using methods spanning the range from femtosecond spectroscopy and crystallography to biochemistry and molecular biology. Here, we focus on the structural basis for the function of this protein, with primary emphasis on the contributions of electron microscopy and crystallography towards unravelling the mechanism of vectorial proton pumping.
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