ISSN:
0021-8995
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
,
Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
,
Physics
Notes:
Fourier transform infrared spectroscopy (FTIR) was employed to explore the structural transformation by stretching of the film composed of a keratin derivative. The derivative was prepared by S-carboxymethylation of the low-sulfur keratin of wool. The cast film was stretched to different ratios in ethanol/water (7:3 v/v). The amide infrared absorption bands of the derivative were changed by stretching the film. Curve analysis was undertaken to estimate the contribution of each peptide conformation to the amide II band at each stretching. The analysis shows that the stretching mainly causes the structural transformation from random coil to β-structure. Moreover, a transient state arises in the course of the transformation. In such a state, the part of random coil increases while that of β-structure decreases. The infrared dichroism of the film also supports the existence of the transient state. On curve analysis, only the α-structure was found to reverse the dichroism of the amide II band in the transient state. This result suggests that the crystalline phase of α-structure is rearranged. Such rearrangement results in inhibition of the transformation from random coil to β-structure.
Additional Material:
8 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/app.1989.070370805
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