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Spontaneous unwinding
of a labile domain in a collagen triple helix
Krishnakumar M. Ravikumar, Jay D. Humphrey and Wonmuk Hwang |
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Vol. 2 (2007), No. 6, 999–1010
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Abstract |
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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. |
Keywords
collagen, cleavage, unwinding, lability, microunfolding
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Milestones
Received: 12 September 2006
Accepted: 20 December 2006
Published: 1 August 2007
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Authors |
| Krishnakumar M. Ravikumar | |
| Department of Biomedical
Engineering Texas A&M University College Station, Texas 77843-3120 United States |
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| Jay D. Humphrey | |
| Department of Biomedical
Engineering Texas A&M University College Station, Texas 77843-3120 United States |
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| Wonmuk Hwang | |
| Department of Biomedical
Engineering Texas A&M University College Station, Texas 77843-3120 United States |
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