作者
Anne George, Arthur Veis
发表日期
1991/3/1
期刊
Biochemistry
卷号
30
期号
9
页码范围
2372-2377
出版商
American Chemical Society
简介
Revised Manuscript Received November 30, 1990 abstract: The assembly of type I collagen molecules into native fibrils can be accomplished in vitro in solutions at physiological ionic strength and pH by raising the temperature above30 C. The thermal self-assembly reaction exhibits a distinct lag phase. This lag phase has been proposed to be evidence for a conformational transition in the monomer. Fourier transform infrared spectroscopy (FTIRS) is a very sensitive probe of the H-bonded states within the triple helix. The carbonyl group spectrum (amideI, 1700-1600 cm'1) has been investigated in collagen/H20 solutions at 1 mg/mL under self-assembly conditions from 4 to 34 C and, in the same range, at a higher ionic strength where self-assembly does not occur. The deconvoluted spectra show three very clear bands at «1660, 1644, and 1630 cm'1. These bands vary in both frequency maxima and relative …
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