Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 102, Issue 38, Pages 13457-13460Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0506864102
Keywords
collagen; helix; optical rotation; gelatin; chirality
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Funding
- Engineering and Physical Sciences Research Council [GR/S61263/01] Funding Source: researchfish
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By combining dynamic mechanical and optical measurements in probing the internal structure of a biopolymer network (gelatin gel), we studied the quasi-equilibrium evolution of helical content as a function of the applied stress. Assuming that the net optical activity is proportional to the concentration of secondary helices of collagen chains, and assuming that affine mechanical deformation, we find a nonmonotonic relationship between the helical domains and an imposed deformation. The results are in qualitative agreement with theoretical predictions of alpha-helices induced by chain end-to-end stretching, and give a consistent picture of mechanically stimulated helix-coil transition in networks of denatured polypeptides.
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