Induced helicity in biopolymer networks under stress.
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.
Courty
S
S
Cavendish Laboratory, University of Cambridge, Madingley Road, Cambridge CB3 0HE, United Kingdom.
Gornall
J L
JL
Terentjev
E M
EM
D001704:Biopolymers / Q000737:chemistry*; D005780:Gelatin / Q000737:chemistry*; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D013314:Stress, Mechanical
D001704:Biopolymers; D005780:Gelatin