Spontaneous unwinding of a labile domain in a collagen triple helix Academic Article

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.

authors

• Hwang, Wonmuk

published proceedings

• JOURNAL OF MECHANICS OF MATERIALS AND STRUCTURES

author list (cited authors)

• Ravikumar, K. M., Humphrey, J. D., & Hwang, W.

citation count

• 16

complete list of authors

• Ravikumar, Krishnakumar M||Humphrey, Jay D||Hwang, Wonmuk

publication date

• January 2007

publisher

• Mathematical Sciences Publishers  Publisher

published in

• Journal of Mechanics of Materials and Structures  Journal

keywords

• Cleavage
• Collagen
• Lability
• Microunfolding
• Unwinding

Digital Object Identifier (DOI)

• 10.2140/jomms.2007.2.999

start page

• 999

end page

• 1010

volume

• 2

issue

• 6

URL

• http%3A%2F%2Fdx.doi.org%2F10.2140%2Fjomms.2007.2.999