Abstract
Measurements of infrared spectra obtained with polarized radiation are reported for nylon, silk fibroin, feather rachis, stretched wool, and kangaroo tail tendon before and after reaction with deuterium oxide. In every case except tendon replacement of hydrogen by deuterium in the peptide linkage occurs preferentially in the less well oriented regions of the specimen. A residual absorption band between 4600 and 4650 cm—1 is evident in the partially deuterated protein specimens and it is suggested that this may be assigned to a combination of CH and CO stretching modes.
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Dates
Type | When |
---|---|
Created | 20 years, 7 months ago (Jan. 5, 2005, 9:16 p.m.) |
Deposited | 1 year, 6 months ago (Feb. 8, 2024, 1:52 p.m.) |
Indexed | 11 months, 3 weeks ago (Sept. 10, 2024, 10:35 p.m.) |
Issued | 66 years, 10 months ago (Nov. 1, 1958) |
Published | 66 years, 10 months ago (Nov. 1, 1958) |
Published Print | 66 years, 10 months ago (Nov. 1, 1958) |
@article{Fraser_1958, title={Hydrogen →Deuterium Exchange Reaction in Fibrous Proteins. I}, volume={29}, ISSN={1089-7690}, url={http://dx.doi.org/10.1063/1.1744648}, DOI={10.1063/1.1744648}, number={5}, journal={The Journal of Chemical Physics}, publisher={AIP Publishing}, author={Fraser, R. D. B. and MacRae, T. P.}, year={1958}, month=nov, pages={1024–1028} }