Hydrogen →Deuterium Exchange Reaction in Fibrous Proteins. I

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.