Spontaneous unwinding of a labile domain in a collagen triple helix
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We have analyzed thermal unwinding behavior of a biologically relevant collagen mimetic peptide (PDB ID): 1bkv) through molecular dynamics simulations in explicit water. Conformational changes of the triple helix were monitored by introducing a set of local triad vectors and measuring variations in their torsional angles. Although the molecule fluctuates thermally at 273 K, unwinding becomes pronounced at 300 K and 330 K. We found that the region containing Gly-Ile, which is a common cleavage site in collagen, to be an initiation site for unwinding. Our results suggest that local unwinding of collagen is spontaneous at physiological temperatures, and it could be a property utilized for binding by other proteins, such as cleavage enzymes or fibril associated collagens.
author list (cited authors)
Ravikumar, K., Humphrey, J., & Hwang, W.