PMID: 8612612Mar 1, 1996Paper

A note on circular-dichroic-constrained prediction of protein secondary structure

European Journal of Biochemistry
A Galat

Abstract

Circular dichroic (CD) spectra of bovine immunosuppressant binding proteins FKBP12 and FKBP25, and cyclophilins (peptidylprolyl isomerases) A (bCyP-18) and B(bCyP-20), the immunophilins which selectively bind the clinically useful immunosuppressants FK506, rapamycin and cyclosporin A, respectively, were analysed using the singular-value-decomposition algorithm augmented by a simplified variable selection method. The differences between the CD-estimated values of alpha-helix, beta-structure and beta-turn and those predicted by the Chou-Fasman algorithm were minimized using the CD data as constraints of an algorithm which utilizes the method of hierarchical updating of quasi-equipotential peptide segments of the Chou-Fasman prediction. The method allows one to correct the Chou-Fasman prediction of secondary structures in globular proteins.

References

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Citations

Dec 7, 2000·Journal of Computational Biology : a Journal of Computational Molecular Cell Biology·C Bailey-KelloggB R Donald
Aug 8, 1997·Biochemical and Biophysical Research Communications·A Galat, F Bouet
Jun 1, 2014·International Journal of Biological Macromolecules·Andrzej GalatEnrico A Stura
Jun 15, 1997·Analytical Chemistry·A F HühmerC Schôneich

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