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Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
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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Metadata
- Authors
- Whitmore, L., & Wallace, B. A.
- Venue
- Biopolymers
- Publisher
- Wiley
- Published
- 2007-09-25
- Volume
- 89
- Issue
- 5
- Pages
- 392-400
- ISSN
- 0006-3525 (ISSN-L)
- 1097-0282
- OpenAlex
- W2026727321
- Cited by
- 2,243
- References
- 0
- FWCI
- 17.84
- Type
- journal article
- Language
- en
- Open access
- closed
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