Direct quantification of the flexibility of type I collagen monomer.

Abstract:

:Collagens are the most abundant structural proteins found in the extracellular matrix of vertebrates. Knowledge of the mechanical behavior of collagen monomers is essential for understanding the mechanical properties of collagen fibrils that constitute the main architectural framework of skin, bone, cartilage, and other connective tissues. In this study, the flexibility of type I collagen monomer was studied by stretching type I collagen monomers directly. The force-extension relationship was measured and analyzed by fitting the data into a worm-like chain elasticity model. The persistence length of collagen I monomer was determined to be 14.5 nm and the contour length was 309 nm. The results confirm that type I collagen monomer is flexible rather than rigid, rod-like molecule. Such flexibility may possibly be a consequence of the micro-unfolding of discrete domains of single collagen molecule.

authors

Sun YL,Luo ZP,Fertala A,An KN

doi

10.1016/s0006-291x(02)00685-x

subject

Has Abstract

pub_date

2002-07-12 00:00:00

pages

382-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X0200685X

journal_volume

295

pub_type

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