title: Use of EPR spectroscopy to study macromolecular structure and function.
abstract: Electron paramagnetic resonance (EPR) spectroscopy is now part of the armory available to probe the structural aspects of proteins, nucleic acids and protein-nucleic acid complexes. Since the mobility of a spin label covalently attached to a macromolecule is influenced by its microenvironment, analysis of the EPR spectra of site-specifically incorporated spin labels (probes) provides a powerful tool for investigating structure-function correlates in biological macromolecules. This technique has become readily amenable to address various problems in biology in large measure due to the advent of techniques like site-directed mutagenesis, which enables site-specific substitution of cysteine residues in proteins, and the commercial availability of thiol-specific spin-labeling reagents (Figure 1). In addition to the underlying principle and the experimental strategy, several recent applications are discussed in this review.
authors.affiliation: Department of Biochemistry, Ohio State University, Columbus, OH 43210-1292, USA.
authors.forename: R
authors.initials: R
authors.lastname: Biswas
authors.forename: H
authors.initials: H
authors.lastname: Kühne
authors.forename: G W
authors.initials: GW
authors.lastname: Brudvig
authors.forename: V
authors.initials: V
authors.lastname: Gopalan
mesh_terms: D000818:Animals; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D016297:Mutagenesis, Site-Directed; D020836:Protein Structure, Quaternary; D013113:Spin Labels
chemical_list: D013113:Spin Labels