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Title of Journal: Amino Acids

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Abbravation: Amino Acids

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Springer-Verlag

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DOI

10.1007/bf02398744

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1438-2199

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Circular dichroism and crosslinking studies of ba

Authors: E Karnaukhova K L Schey R K Crouch
Publish Date: 2006/02/15
Volume: 30, Issue: 1, Pages: 17-23
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Abstract

Circular dichroism CD spectroscopy was employed for native wild type WT bacteriorhodopsin bR and several mutant derivatives R134K R134H R82Q S35C L66C and R134C/E194C Comparative analysis of the CD spectra in visible range shows that only R134C/E194C exhibits biphasic CD typical for native bR the other mutants demonstrate CD spectra with significantly smaller or absent negative band Since the biphasic CD is a feature of hexagonal lattice structure composed by bR trimers in the purple membrane these mutants and WT were examined by crosslinking studies which confirmed the same trend towards trimeric organization Therefore a single amino acid substitution may lead to drastically different CD spectra without disruption of bR trimeric organization Thus although disruption of bR trimeric crystalline lattice structure eg solubilization with detergents directly results in the disappearance of characteristic bilobe in visible CD the lack of the bilobe in the CD alone does not predict the absence of trimers

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