| Literature DB >> 6838964 |
Abstract
A simple model is presented for the motion of phenylalanine and tyrosine rings in proteins. The model consists of restricted rotational diffusion of the rings about the side chain C alpha--C beta (chi 1) and C beta--C gamma (chi 2) axes combined with 180 degree ring flips. The model is used to evaluate order parameters for nuclear magnetic resonance relaxation and fluorescence depolarization probes of aromatic ring motions in proteins. The dependence of the order parameters on orientation in the ring plane is examined and it is demonstrated that in the presence of ring flips, additional ring librations can have a large effect on the probe order parameters.Entities:
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Year: 1983 PMID: 6838964 PMCID: PMC1329169 DOI: 10.1016/S0006-3495(83)84422-1
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033