Secondary structure of streptokinase in aqueous solution - a fourier transform infrared spectroscopic study

Item Type:	Article
Title:	Secondary structure of streptokinase in aqueous solution - a fourier transform infrared spectroscopic study
Creators Name:	Fabian, H. and Naumann, D. and Misselwitz, R. and Ristau, O. and Gerlach, D. and Welfle, H.
Abstract:	The secondary structure of streptokinase (Sk) in aqueous solution was quantitatively examined by using Fourier transform infrared (FT-IR) spectroscopy. Resolution enhancement techniques, including Fourier deconvolution and derivative spectroscopy, were combined with band curve-fitting procedures to quantitate the spectral information from the amide I bands. Nine component bands were found under the broad, nearly featureless amide I bands which reflect the presence of various substructures. The relative areas of these component bands indicate an amount of beta-sheet between 30 and 37% and an alpha-helix content of only 12-13% in Sk. Further conformational substructures are assigned to turns (25-26%) and to "random" structures (15-16%). Additionally, the correlation of a pronounced component band near 1640 cm-1 (10-16% fractional area) with the possible presence of 3(10)-helices is discussed.
Keywords:	Amides, Deuterium, Fourier Analysis, Hydrogen Bonding, Infrared Spectrophotometry, Protein Conformation, Streptokinase, Water
Source:	Biochemistry
ISSN:	0006-2960
Publisher:	American Chemical Society
Volume:	31
Number:	28
Page Range:	6532-6538
Date:	21 July 1992
Official Publication:	https://doi.org/10.1021/bi00143a023
PubMed:	View item in PubMed

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