Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set.

By Narasimha Sreerama, Robert W. Woody. Analytical Biochemistry, 2000

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Subfields: Gender Studies, Political Science and International Relations

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Citations in the corpus

Characterisation of acid protease expressed from Aspergillus oryzae MTCC 5341 (2009, methodology): “Secondary structure analysis was carried out using the CDSSTR method (Compton & Johnson, 1986; Sreerama & Woody, 2000) with reference database SP175 (Lees, Miles, Wien, & Wallace, 2006) available in DICHROWEB (Lobley, Whitmore, & Wallace, 2002).”
Structural composition of βI‐ and βII‐proteins (2003, methodology): “Despite the two classes of CD spectra for -rich proteins, the performance of the CD analysis for estimating -sheet content is quite reasonable ( ∼ 9% RMS deviation between x-ray and CD estimates; Sreerama and Woody 2000b).”
DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra (2002, background): “Data analyses can be done using a number of the most popular secondary structure determination algorithms, including SELCON3 (Sreerama and Woody, 1993; Sreerama et al., 1999), CONTIN (Provencher and Glockner, 1981; Van Stokkum et al., 1990), VARSLC (Compton and Johnson, 1986; Manavalan and Johnson, ”
Estimation of the number of α‐helical and β‐strand segments in proteins using circular dichroism spectroscopy (2008, methodology): “…protein secondary structures~Greenfield & Fasman, 1969; Chen & Yang, 1971; Bolotina et al., 1980; Brahms & Brahms, 1980; Hennessey & Johnson, 1981; Provencher & Glöckner, 1981; Manavalan & Johnson, 1987; Shubin et al., 1990; van Stokkum et al., 1990; Pancoska et al., 1991; Perczel et al., 1991;…”
A general amphipathic α-helical motif for sensing membrane curvature (2007, methodology): “The spectra were analyzed in the 200−240 nm range with CDPr”