Abstract
Publisher Summary This chapter discusses the ultraviolet circular dichroism (CD) of rhodopsin in disk membranes and detergent solution. The ultraviolet CD of proteins is dominated by the contributions of the peptide group. The magnitude, sign, and position of the peptide circular dichroic bands are sensitive to the secondary folding of the polypeptide backbone. Analysis of this region of the CD spectrum is the most direct method of estimating the secondary structure of proteins in solution and has been used successfully with soluble globular proteins. However, the structural analysis of membrane proteins has produced ambiguous results, because of certain anomalies that are observed in the CD spectra of such samples; these are characterized by a red shift and loss of intensity in the peptide cotton effects, which is attributable to the particulate nature of the membrane suspensions.
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