title: Solvent specific persistence length of molecular type I collagen.
abstract: 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.
authors.affiliation: Department of Physics, University of South Florida, Tampa, FL, 33620-5700.
authors.forename: Heather H
authors.initials: HH
authors.lastname: Lovelady
authors.forename: Satish
authors.initials: S
authors.lastname: Shashidhara
authors.forename: W Garrett
authors.initials: WG
authors.lastname: Matthews
mesh_terms: D000818:Animals; D002021:Buffers; D002417:Cattle; D024042:Collagen Type I / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D053758:Nanoparticles / Q000737:chemistry; D012997:Solvents / Q000737:chemistry*; D014867:Water / Q000737:chemistry
chemical_list: D002021:Buffers; D024042:Collagen Type I; D012997:Solvents; D014867:Water
keywords: atomic force microscopy; collagen; extracellular matrix; molecular mechanics