Abstract
2H-nuclear magnetic resonance (NMR) has been used to study the dynamics of amino acid residues in bacteriorhodopsin with results that depend on the method of sample preparation. We show here that in [2H]-leucine-labeled samples the intensity of the isotropic signal varies according to the degree of residual contamination of the sample with red membrane. We conclude that few of the surface leucine residues of bacteriorhodopsin are moving isotropically on the 2H-NMR time scale.
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Selected References
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