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DICHROWEB, an Online Server for Protein Secondary Structure Analyses from Circular Dichroism Spectroscopic Data

Overview
Specialty Biochemistry
Date 2004 Jun 25
PMID 15215473
Citations 825
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Abstract

The DICHROWEB web server enables on-line analyses of circular dichroism (CD) spectroscopic data, providing calculated secondary structure content and graphical analyses comparing calculated structures and experimental data. The server is located at http://www.cryst.bbk.ac.uk/cdweb and may be accessed via a password-limited user ID, available upon completion of a registration form. The server facilitates analyses using five popular algorithms and (currently) seven different reference databases by accepting data in a user-friendly manner in a wide range of formats, including those output by both commercial CD instruments and synchrotron radiation-based circular dichroism beamlines, as well as those produced by spectral processing software packages. It produces as output calculated secondary structures, a goodness-of-fit parameter for the analyses, and tabular and graphical displays of experimental, calculated and difference spectra. The web pages associated with the server provide information on CD spectroscopic methods and terms, literature references and aids for interpreting the analysis results.

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References
1.
Mao D, Wachter E, Wallace B . Folding of the mitochondrial proton adenosinetriphosphatase proteolipid channel in phospholipid vesicles. Biochemistry. 1982; 21(20):4960-8. DOI: 10.1021/bi00263a020. View

2.
Cascio M, Gogol E, Wallace B . The secondary structure of gap junctions. Influence of isolation methods and proteolysis. J Biol Chem. 1990; 265(4):2358-64. View

3.
Sreerama N, Woody R . A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem. 1993; 209(1):32-44. DOI: 10.1006/abio.1993.1079. View

4.
Provencher S, Glockner J . Estimation of globular protein secondary structure from circular dichroism. Biochemistry. 1981; 20(1):33-7. DOI: 10.1021/bi00504a006. View

5.
Sreerama N, Venyaminov S, Woody R . Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal Biochem. 2000; 287(2):243-51. DOI: 10.1006/abio.2000.4879. View