title: Watching proteins move using site-directed spin labeling.
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.
authors.affiliation: Jules Stein Eye Institute, University of California at Los Angeles 90095-7008, USA. hubbellw@jsei.ucla.edu
authors.forename: W L
authors.initials: WL
authors.lastname: Hubbell
authors.forename: H S
authors.initials: HS
authors.lastname: Mchaourab
authors.forename: C
authors.initials: C
authors.lastname: Altenbach
authors.forename: M A
authors.initials: MA
authors.lastname: Lietzow
mesh_terms: 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
chemical_list: D011506:Proteins; D012997:Solvents; D013113:Spin Labels; D009569:Nitric Oxide