Vol. 2, No. 6, 2007

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ISSN: 1559-3959
Spontaneous unwinding of a labile domain in a collagen triple helix

Krishnakumar M. Ravikumar, Jay D. Humphrey and Wonmuk Hwang

Vol. 2 (2007), No. 6, 999–1010
Abstract

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.

Keywords
collagen, cleavage, unwinding, lability, microunfolding
Milestones
Received: 12 September 2006
Accepted: 20 December 2006
Published: 1 August 2007
Authors
Krishnakumar M. Ravikumar
Department of Biomedical Engineering
Texas A&M University
College Station, Texas 77843-3120
United States
Jay D. Humphrey
Department of Biomedical Engineering
Texas A&M University
College Station, Texas 77843-3120
United States
Wonmuk Hwang
Department of Biomedical Engineering
Texas A&M University
College Station, Texas 77843-3120
United States