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

• Published in: Biopolymers 2008-05, Vol.89 (5), p.392-400
• Main Authors: Whitmore, Lee, Wallace, B. A.
• Format: Article
• Language: English
• Subjects: analyses; bioinformatics; Circular Dichroism - methods; Circular Dichroism - trends; circular dichroism spectroscopy; Databases, Protein - standards; Molecular Structure; protein secondary structure; Protein Structure, Secondary; reference database; Reference Standards; Software; synchrotron radiation circular dichroism (SRCD)
• ISSN: 0006-3525; 1097-0282
• DOI: 10.1002/bip.20853

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 [e-mail]