Biophysical Journal 74: 192-198 (1998)
© 1998 the Biophysical Society

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Biophys J, January 1998, p. 192-198, Vol. 74, No. 1

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

 ^*Department of Physics and Molecular Biophysics Laboratory, Boston University, Boston, Massachusetts 02215 USA and  ^#Department of Biochemistry, Institute of Cellular Signalling, University of Nijmegen, 6500 HB, Nijmegen, The Netherlands

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°C consists of fast (time constant ~30 min) and slow (~11 h) components. These results indicate that photoactivation causes buried portions of the rhodopsin backbone structure to become more accessible.

Biophys J, January 1998, p. 192-198, Vol. 74, No. 1
© 1998 by the Biophysical Society   0006-3495/98/01/192/07  $2.00

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