Watching proteins move using site-directed spin labeling.
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.
Hubbell
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Jules Stein Eye Institute, University of California at Los Angeles 90095-7008, USA. hubbellw@jsei.ucla.edu
Mchaourab
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Altenbach
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Lietzow
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MA
D004578:Electron Spin Resonance Spectroscopy; D009569:Nitric Oxide / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012997:Solvents; D013113:Spin Labels
D011506:Proteins; D012997:Solvents; D013113:Spin Labels; D009569:Nitric Oxide