Use of EPR spectroscopy to study macromolecular structure and function.

R. Biswas, H. Kühne, Gary W Brudvig, V. Gopalan

Research output: Contribution to journalArticle

29 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)45-67
Number of pages23
JournalScience Progress
Volume84
Issue numberPt 1
Publication statusPublished - 2001

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ASJC Scopus subject areas

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