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Spectroscopic Technique for Studying Protein Rotation in Membranes

Nature New Biology volume 245, pages 249–251 (1973)Cite this article

Abstract

DETAILS of the dynamics and mutual interactions of the constituents of cell membranes are now becoming available1. That proteins may have considerable translational mobility in the plane of the membrane was first demonstrated by Frye and Edidin2. Subsequently, Cone3, using flash illumination, studied the transient dichroism of photoproducts of rhodopsin in rod outer segment membranes. He exploited the rapid absorption changes which result from the illumination of the rhodopsin molecule and concluded that rhodopsin was rotating rapidly with a relaxation time of about 20 µs. It is clearly of interest to develop a general method whereby the rotation of other membrane proteins may be investigated.

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References

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Authors and Affiliations

  1. Department of Chemistry, The University, Sheffield, S3 7HF

    K. RAZI NAQVI, J. GONZALEZ-RODRIGUEZ, R. J. CHERRY & D. CHAPMAN

Authors
  1. K. RAZI NAQVI
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  2. J. GONZALEZ-RODRIGUEZ
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  3. R. J. CHERRY
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  4. D. CHAPMAN
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NAQVI, K., GONZALEZ-RODRIGUEZ, J., CHERRY, R. et al. Spectroscopic Technique for Studying Protein Rotation in Membranes. Nature New Biology 245, 249–251 (1973). https://doi.org/10.1038/newbio245249a0

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  • DOI: https://doi.org/10.1038/newbio245249a0

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