Photoactivation of Rhodopsin Causes an Increased Hydrogen-deuterium Exchange of Buried Peptide Groups

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 1998 Feb 4

PMID 9449322

Citations 9

Authors

P Rath

W J Degrip

K J Rothschild

Affiliations

Soon will be listed here.

Abstract

A key step in visual transduction is the light-induced conformational changes of rhodopsin that lead to binding and activation of the G-protein transducin. In order to explore the nature of these conformational changes, time-resolved Fourier transform infrared spectroscopy was used to measure the kinetics of hydrogen/deuterium exchange in rhodopsin upon photoexcitation. The extent of hydrogen/deuterium exchange of backbone peptide groups can be monitored by measuring the integrated intensity of the amide II and amide II' bands. When rhodopsin films are exposed to D2O in the dark for long periods, the amide II band retains at least 60% of its integrated intensity, reflecting a core of backbone peptide groups that are resistant to H/D exchange. Upon photoactivation, rhodopsin in the presence of D2O exhibits a new phase of H/D exchange which at 10 degrees C consists of fast (time constant approximately 30 min) and slow (approximately 11 h) components. These results indicate that photoactivation causes buried portions of the rhodopsin backbone structure to become more accessible.

Citing Articles

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