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Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases †

  1. Lee Whitmore,
  2. B. A. Wallace*

Article first published online: 25 SEP 2007

DOI: 10.1002/bip.20853

Issue

Biopolymers

Biopolymers

Special Issue: This issue is dedicated to the memory of Elkan R. Blout, a founding editor of Biopolymers

Volume 89, Issue 5, pages 392–400, May 2008

Additional Information

How to Cite

Whitmore, L. and Wallace, B. A. (2008), Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases . Biopolymers, 89: 392–400. doi: 10.1002/bip.20853

Author Information

  1. Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX, UK

*Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX, UK

  1. †

    This article is dedicated to the memory of Elkan R. Blout, in whose lab BAW was first introduced to CD spectroscopy as a postdoc.

Publication History

  1. Issue published online: 28 FEB 2008
  2. Article first published online: 25 SEP 2007
  3. Manuscript Accepted: 17 SEP 2007
  4. Manuscript Revised: 13 SEP 2007
  5. Manuscript Received: 9 AUG 2007

Funded by

  • Biotechnology and Biological Sciences Research Council

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Keywords:

  • circular dichroism spectroscopy;
  • protein secondary structure;
  • analyses;
  • reference database;
  • bioinformatics;
  • synchrotron radiation circular dichroism (SRCD)

Abstract

Circular dichroism (CD) spectroscopy has been a valuable method for the analysis of protein secondary structures for many years. With the advent of synchrotron radiation circular dichroism (SRCD) and improvements in instrumentation for conventional CD, lower wavelength data are obtainable and the information content of the spectra increased. In addition, new computation and bioinformatics methods have been developed and new reference databases have been created, which greatly improve and facilitate the analyses of CD spectra. This article discusses recent developments in the analysis of protein secondary structures, including features of the DICHROWEB analysis webserver. © 2007 Wiley Periodicals, Inc. Biopolymers 89: 392–400, 2008.

This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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