The CD-ProWin7 is a software package for quantitative analysis of Circular Dichroism spectra from proteins and peptides. Inside this package one can find the programs SELCONWin7, CDSSTRWin7 and CONTINLLWin7 which are upgrades and small corrections of SELCON3, CDSSTR and CONTINLL originally developed by professors’ Robert W. Woody and N. Sreerama group. The upgrade and correction were done by Professor’s Patricia Targon Campana group with the professor’s Woody agreement. The complete references can be found at the bottom of this page and also inside the programs.

A bit of each program

SELCON

Selcon was developed at professor’s Robert W. Woody lab and it is based on Singular Value Decomposition method of CD spectrum. In this method, the experimental spectrum is transformed into a matrix which is added as new lines to the matrix that contains the secondary structures for reference (base, from W.C. Johnson Jr). The method Locally Linearized (van Stokkum et al) is also utilized for the method implementation.

CONTIN LL

O CONTIN LL is a variation developed by Provencher e Glöckner (CONTIN). The CONTIN program was developed at 80’ and has a general proposal to solve integral equations and algebraic linear systems. The software is called CONTIN because it applies solutions for first degree integrals and does the continuous distributions of diffusion coefficients.

CDSSTR

Developed by W. C. Johnston, the CDSSTR is a modification of VARSLC (Variable Selection) method, which utilized all possible combinations of a fixed number of proteins. This method is, generally, the most precise, but is also the slowest due to the number of the executed calculations.

References

Pastor J., Bíscaro H.H. and Campana P.T. 2014. CDPro2: CDPro CD spectra deconvolution programs upgraded. Download available at: (endereço do aprender ciência).

SREERAMA, N.; WOODY, R.W. A Self-Consistent Method for the analysis of Protein Secondary Structure from Circular Dichroism. Analytical Biochemistry 209: 32-44, 1993.

SREERAMA, N.; WOODY, R.W. Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J. Mol. Biol. 242:497-507, 1994.

SREERAMA, N.; VENYAMINOV, S. Y.; WOODY, R.W. Estimation of the number of a-helical and b-strand segments in proteins using CD spectroscopy. Protein Science, 8: 370-380, 1999.

SREERAMA, N.; VENYAMINOV, S. Y.; WOODY, R.W. Estimation of protein secondary structure from CD spectra: Inclusion of denatured proteins with native protein in the analysis. Analytical Biochemistry 287: 243-251, 2000.

SREERAMA, N.; WOODY, R. W. Estimation of Protein Secondary Structure from Circular Dichroism Spectra: Comparison of CONTIN, SELCON, and CDSSTR Methods with an Expanded Reference Set. Analytical Biochemistry 287: 252–260, 2000.

PROVENCHER, W. S.; GLOCKNER, J. Estimation of protein secondary structure from circular dichroism. Biochemistry 20: 33-37, 1981.

PROVENCHER, W. S. Technical Report EMBL-DA07, 1984. Disponível em http://S-provencher.com

HENNESSEY, J. P.; JOHNSON, W. C.. Information Content in the Circular Dichroism of Proteins. Biochemistry, 20, 1085-1094, 1981.

JOHNSON, W. C.. Analyzing Protein CD for Accurate secondary Structures. Proteins: Structure, Function, and Genetics 35: 307-312, 1999.