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.
Cited by
144 articles.
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