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Nuclear magnetic resonance studies on the structure and function of rhodopsin

Published online by Cambridge University Press:  04 February 2010

Steven O. Smith*
Affiliation:
Department of Molecular Biophysics and Biochemistry, Yale University, Box 208114, New Haven, CT 06520. smith@loki.csb.yale.edu

Abstract

Magic angle spinning (MAS) NMR methods provide a means of obtaining high resolution structural data on rhodopsin and its photoin termediates. Current work has focused on the structure of the retinal chromophore and its interactions with surrounding protein charges. The recent development of MAS NMR methods for measuring internuclear distances with a resolution of ∼0.2 will complement diffraction methods for addressing key mechanistic questions.

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Copyright
Copyright © Cambridge University Press 1995

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