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Convex Constraint Decomposition of Circular Dichroism Curves of Proteins

Andras Perczel ; The Department of Organic Chemistry, L. Eotvos University, P.O.B. 325, H-1445 Budapest, Hungary
Miklos Hollosi ; The Department of Organic Chemistry, L. Eotvos University, P.O.B. 325, H-1445 Budapest, Hungary
Gabor Tusnady ; Mathematical Institute of the Hungarian Academy of Sciences, Budapest, Hungary
Gerald D. Fasman ; Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254

Puni tekst: engleski, pdf (4 MB) str. 189-200 preuzimanja: 76* citiraj
APA 6th Edition
Perczel, A., Hollosi, M., Tusnady, G. i Fasman, G.D. (1989). Convex Constraint Decomposition of Circular Dichroism Curves of Proteins. Croatica Chemica Acta, 62 (2A), 189-200. Preuzeto s https://hrcak.srce.hr/175392
MLA 8th Edition
Perczel, Andras, et al. "Convex Constraint Decomposition of Circular Dichroism Curves of Proteins." Croatica Chemica Acta, vol. 62, br. 2A, 1989, str. 189-200. https://hrcak.srce.hr/175392. Citirano 22.01.2021.
Chicago 17th Edition
Perczel, Andras, Miklos Hollosi, Gabor Tusnady i Gerald D. Fasman. "Convex Constraint Decomposition of Circular Dichroism Curves of Proteins." Croatica Chemica Acta 62, br. 2A (1989): 189-200. https://hrcak.srce.hr/175392
Harvard
Perczel, A., et al. (1989). 'Convex Constraint Decomposition of Circular Dichroism Curves of Proteins', Croatica Chemica Acta, 62(2A), str. 189-200. Preuzeto s: https://hrcak.srce.hr/175392 (Datum pristupa: 22.01.2021.)
Vancouver
Perczel A, Hollosi M, Tusnady G, Fasman GD. Convex Constraint Decomposition of Circular Dichroism Curves of Proteins. Croatica Chemica Acta [Internet]. 1989 [pristupljeno 22.01.2021.];62(2A):189-200. Dostupno na: https://hrcak.srce.hr/175392
IEEE
A. Perczel, M. Hollosi, G. Tusnady i G.D. Fasman, "Convex Constraint Decomposition of Circular Dichroism Curves of Proteins", Croatica Chemica Acta, vol.62, br. 2A, str. 189-200, 1989. [Online]. Dostupno na: https://hrcak.srce.hr/175392. [Citirano: 22.01.2021.]

Sažetak
A new algorithm, called convex analysis, has been developed
to deduce the chiral contribution of the common secondary structures
directly from experimental circular dichroism (CD) curves
of a large number of proteins. The analysis is based on CD data
reported by Yang et aU Test runs were performed on sets of artificial
protein spectra created by the Monte Carlo technique using
poly-u-Iysine based component spectra. Application of the decomposition algorithm for the created sets of spectra resulted in
component spectra [B (2, i)] and weights [C (i, k)] with excellent
Pearson correlation coefficients (r).2 The algori thm, independent
of X-ray data, revealed that the CD spectrum of a given protein
is composed of at least four independent sources of chirality. Three
of the computed component curves show remarkable resemblance
to the CD spectra of known protein secondary structures. This
approach yields a significant improvement compared to the eigenvector analysis of Hennessey and Johnson." The new method is a useful tool not only in analyzing CD spectra but also in treating
other decomposition problems where an additivity constraint is
valid.

Hrčak ID: 175392

URI
https://hrcak.srce.hr/175392

Posjeta: 152 *