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Determination of the secondary structures of proteins by circular dichroism spectra. Calculation of the protein basic circular dichroism spectra for antiparallel and parallel β-structures and β-bends

✍ Scribed by I. A. Bolotina; V. O. Chekhov; V. Yu. Lugauskas

Publisher
John Wiley and Sons
Year
1979
Tongue
English
Weight
344 KB
Volume
16
Category
Article
ISSN
0020-7608

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✦ Synopsis

Abstract

New “reference” circular dichroism spectra of α helix, β‐structure (both parallel and antiparallel), β‐bends, and the unordered form are obtained from circular dichroism spectra and x‐ray data for six proteins (myoglobin, lysozyme, lactate dehydrogenase, papain, ribonuclease, and subtilisin BPN′). Circular dichroism spectra for α‐helix and antiparallel β‐structure are similar to those for poly(Llysine). The circular dichroism spectrum of the parallel β‐structure is qualitatively similar to that theoretically calculated by Madison and Schellman. The circular dichroism spectrum of β‐bends is qualitatively similar to that theoretically calculated by Woody. The spectrum of the unordered form is close to that of the denaturated proteins. These “reference” circular dichroism spectra used for the analysis of the secondary structure of ten globular proteins (besides the six reference proteins D‐glyceraldehyde 3‐phosphate dehydrogenase, concanavalin A, cytochrome c, and insulin).

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