Infra-red spectra and structure of fibrous proteins

Abstract

Abstract The spectra of silk suture, porcupine quill, elephant hair, swan quill, gelatine and rat-tail tendon have been observed with polarized infra-red radiation. The first four materials give spectra which show that they contain both extended (β) and folded (α) peptide chains. A band at about 4600 cm.-1 is assigned to a C = O combination frequency, whose dichroism indicates the direction of the transition moment for a C = O deformation mode. Gelatine and collagen give similar spectra, and are different from either α or β proteins or polypeptides. A method of folding a peptide chain, based on a suggestion of Huggins, is given which accounts for the known infra-red and X-ray spectra of collagen and gelatine.