| Literature DB >> 1633164 |
H Fabian1, D Naumann, R Misselwitz, O Ristau, D Gerlach, H Welfle.
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.Entities:
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Year: 1992 PMID： 1633164 DOI： 10.1021/bi00143a024
Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162