Authors: Richard Cammack
Publish Date: 2009/11/12
Volume: 37, Issue: 1-4, Pages: 257-
Abstract
Electron paramagnetic resonance EPR spectroscopy can provide answers to significant questions about structure and function in biochemistry Often EPR spectra of proteins containing transitionmetal centers and radicals show the influence of electron spin–spin interactions between paramagnets Analysis of these spectra provides information about distances and molecular orientations For small proteins the shape of the EPR spectra is sensitive to freezing effects and to changes in the solvent environment intermolecular spin–spin interactions are also observed For large complex proteins details of the EPR spectra are often highly conserved in evolution Reference spectra of paramagnetic proteins are an aid to identification The sharing of data is becoming a requirement in the public funding of research and deposition in public databases is already standard for information such as protein structures and gene sequences This would require the adoption of standard file formats such as JCAMPDX Joint Committee on Atomic and Molecular Physical Data Exchange or Bruker BES3T Bruker EPR Standard for Spectrum Storage and Transfer An archive of EPR spectra of different types of paramagnetic proteins would assist the identification of paramagnetic centers in biological materials It would increase the profile of research data allow comparison of different studies and further interpretation of data in the light of subsequent discoveriesI am grateful to many colleagues over the years for providing advice assistance samples and interesting questions in particular Patrick Bertrand Bruno Guigliarelli Charles Holmes Don Kelly Jeremy Mason Jose and Isobel Moura Krishna Rao Richard Rothery Stephen Seah Jas Shergill Piyush Unalkat and Joel Weiner
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