Non-linearity of the collagen triple helix in solution and implications for collagen function.

ABSTRACT: Collagen adopts a characteristic supercoiled triple helical conformation which requires a repeating (Xaa-Yaa-Gly)_n sequence. Despite the abundance of collagen, a combined experimental and atomistic modelling approach has not so far quantitated the degree of flexibility seen experimentally in the solution structures of collagen triple helices. To address this question, we report an experimental study on the flexibility of varying lengths of collagen triple helical peptides, composed of six, eight, ten and twelve repeats of the most stable Pro-Hyp-Gly (POG) units. In addition, one unblocked peptide, (POG)_10unblocked, was compared with the blocked (POG)₁₀ as a control for the significance of end effects. Complementary analytical ultracentrifugation and synchro

SUBMITTER: Walker KT 

PROVIDER: S-EPMC5632799 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature