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Solvent specific persistence length of molecular type I collagen
Author(s) -
Lovelady Heather H.,
Shashidhara Satish,
Matthews W. Garrett
Publication year - 2014
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22365
Subject(s) - chemistry , persistence (discontinuity) , persistence length , biophysics , organic chemistry , molecule , geotechnical engineering , engineering , biology
Type I collagen is a fibril‐forming protein largely responsible for the mechanical stability of body tissues. The tissue level properties of collagen have been studied for decades, and an increasing number of studies have been performed at the fibril scale. However, the mechanical properties of collagen at the molecular scale are not well established. In the study presented herein, the persistence length of pepsin digested bovine type I collagen is extracted from the conformations assumed when deposited from solution onto two‐dimensional surfaces. This persistence length is a measure of the flexibility of the molecule. Comparison of the results for molecules deposited from different solvents allows for the study of the effect of the solutions on the flexibility of the molecule and provides insight into the molecule's behavior in situ . © 2013 Wiley Periodicals, Inc. Biopolymers 101: 329–335, 2014.