This article is dedicated to the memory of Elkan R. Blout, in whose lab BAW was first introduced to CD spectroscopy as a postdoc.
Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases †
Article first published online: 25 SEP 2007
Copyright © 2008 Wiley Periodicals, Inc.
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
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
- Issue published online: 28 FEB 2008
- Article first published online: 25 SEP 2007
- Manuscript Accepted: 17 SEP 2007
- Manuscript Revised: 13 SEP 2007
- Manuscript Received: 9 AUG 2007
- Biotechnology and Biological Sciences Research Council
- circular dichroism spectroscopy;
- protein secondary structure;
- reference database;
- synchrotron radiation circular dichroism (SRCD)
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 email@example.com