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PubMed · 8805569

Watching proteins move using site-directed spin labeling.

W L Hubbell·H S Mchaourab·C Altenbach·M A Lietzow
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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.

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Electron Spin Resonance SpectroscopyNitric OxideProtein Structure, SecondaryProtein Structure, TertiaryProteinsSolventsSpin LabelsJournal Article

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W L Hubbell, H S Mchaourab, C Altenbach, M A Lietzow. 1996-07-15. Watching proteins move using site-directed spin labeling.. https://doi.org/10.1016/s0969-2126(96)00085-8

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Electron Spin Resonance Spectroscopy↗
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