Monitoring membrane protein rotational diffusion using time-averaged phosphorescence.

E K Murray; C J Restall; D Chapman

doi:10.1016/0005-2736(83)90050-0

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Monitoring membrane protein rotational diffusion using time-averaged phosphorescence.

E K Murray·C J Restall·D Chapman

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Abstract

Rotational motions of membrane proteins have previously been measured using time-dependent phosphorescence techniques. This paper discusses a method of examining membrane protein mobility at temperatures relevant to biological systems, using a technique similar to steady-state fluorescence. The method is demonstrated using sarcoplasmic reticulum ATPase labelled with erythrosin isothiocyanate, both in its natural condition and crosslinked by incubation with glutaraldehyde. The experimentally-observed dependence of phosphorescence anisotropy on temperature is compared to a calculated anisotropy-temperature curve. Comparison is made between the anisotropy decay curves obtained by time-averaged phosphorescence and steady-state fluorescence.

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Animals Diffusion Kinetics Luminescent Measurements Membrane Proteins Microscopy, Fluorescence Muscles Rabbits Sarcoplasmic Reticulum Time Factors Journal Article Research Support, Non-U.S. Gov't

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E K Murray, C J Restall, D Chapman. 1983-07-27. Monitoring membrane protein rotational diffusion using time-averaged phosphorescence.. https://doi.org/10.1016/0005-2736(83)90050-0

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