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

Analytical Biochemistry

Volumn 287, Issue 2, 2000, Pages 252-260

  Sreerama, Narasimha ^a   Woody, Robert W ^a  

^a Veterinary Dentistry and Oral Surgery   (United States)

Author keywords

CD analysis; CDPro software; Protein CD; Protein secondary structure

Indexed keywords

ALGORITHM; ARTICLE; CIRCULAR DICHROISM; COMPUTER PROGRAM; INTERMETHOD COMPARISON; PERFORMANCE; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; RELIABILITY;

EID: 0034672325     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.2000.4880     Document Type: Article

References (36)

1. Computed circular dichroism spectra for the evaluation of protein conformation
2. A new basis for interpreting the circular dichroism spectra of proteins
3. A new approach to the calculation of secondary structures of globular proteins by optical rotatory dispersion and circular dichroism
4. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
5. Determination of the secondary structure of proteins from the circular dichroism spectra. 1. Protein reference spectra for α-, β- and irregular structures
6. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
7. Estimation of protein secondary structure from circular dichroism
8. Information content in the circular dichroism of proteins
9. Variable selection method improves the prediction of protein secondary structure from circular dichroism
10. Prediction of protein secondary structure of globular proteins using circular dichroism spectra
11. Estimation of protein secondary structure and error analysis from circular dichroism spectra
12. Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins
13. Systematic comparison of statistical analysis of electronic and vibrational circular dichroism for secondary structure prediction of selected proteins
14. Quantitative analysis of protein far UV circular dichroism spectra by neural networks
15. A self-consistent method for the analysis of protein secondary structure from circular dichroism
16. Evaluation of secondary structure of protein from UV circular dichroism spectra using unsupervised learning neural network
17. Poly(Pro)II helices in globular proteins: Identification and circular dichroic analysis
18. Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods
19. Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy
20. Analyzing protein circular dichroism spectra for accurate secondary structures
21. Estimation of protein secondary structure from CD spectra: Inclusion of denatured proteins with native proteins in the analysis
22. Calculation of protein conformation from circular dichroism
23. Secondary structure of proteins through circular dichroism spectroscopy
24. Determination of protein secondary structure
25. Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
26. Circular Dichroism of Peptides and Proteins
27. Determination of protein tertiary structure class from circular dichroism spectra
28. Sensitivity of circular dichroism to protein tertiary structure class
29. Circular dichroic analysis of denatured proteins: Inclusion of denatured protein in the reference set
30. Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometric features
31. Comparison of and limits of accuracy for statistical analyses of vibrational and electronic circular dichroism spectra in terms of correlations to and predictions of protein secondary structure
32. Circular dichroism analysis of protein conformation: Inclusion of β-turns
33. Heat capacity and conformation of proteins in the denatured state
34. A constrained regularization method for inverting data represented by linear algebraic or integral equations
35. Assigning secondary structure from protein coordinate data