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Structure. 1996 Jul 15;4(7):779-83.

Watching proteins move using site-directed spin labeling.

Author information

1
Jules Stein Eye Institute, University of California at Los Angeles 90095-7008, USA. hubbellw@jsei.ucla.edu

Abstract

Site-directed spin labeling of proteins has proven to be a practical means for determining secondary structure and its orientation; surfaces of tertiary interactions; inter-residue distances; chain topology and depth of a given side chain from the membrane/aqueous surface in membrane proteins; and local electrostatic potentials at solvent-exposed sites. Moreover, the mobility of a side chain together with its solvent-accessibility may serve to uniquely identify the topographical location of specific residues in the protein fold. Future spectral analysis should permit a quantitative estimation of the contribution of backbone flexibility to the overall side-chain dynamics. The ability to time-resolve the structural features mentioned above makes SDSL a powerful approach for exploring the evolution of structure on the millisecond time scale. We anticipate future applications to the study of protein folding both in solution and in chaperone-mediated systems.

PMID:
8805569
DOI:
10.1016/s0969-2126(96)00085-8
[Indexed for MEDLINE]
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