Premium
Dynamic light‐scattering study of semiflexible polymers: Collagen
Author(s) -
Kubota Kenji,
Tominaga Yasunori,
Fujime Satoru
Publication year - 1987
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.360261006
Subject(s) - radius of gyration , chemistry , dynamic light scattering , gyration , light scattering , diffusion , molecular physics , anisotropy , polymer , scattering , molecule , radius , chain (unit) , momentum transfer , flexibility (engineering) , static light scattering , thermodynamics , physics , optics , quantum mechanics , mathematics , geometry , nanoparticle , computer science , computer security , organic chemistry , statistics
Dynamic light‐scattering measurements were carried out for collagen in acetate buffer (pH 4.8) extracted from lathyritic ratskin. The correlation functions were analyzed in terms of the semiflexibility of collagen molecules. The experimental Γ / K 2 vs K 2 relationship was compared with the theoretical one based on formulation including anisotropy in translational diffusion, chain flexibility, and the hydrodynamic interaction; Γ is the average decay rate and K is the magnitude of the momentum transfer vector. By using the model parameters evaluated from the Γ / K 2 vs K 2 relationship, a good agreement was obtained between profiles of theoretical and experimental correlation functions over the entire delay times. Detailed examinations of the dynamic light‐scattering spectrum permitted us to conclude that a set of the contour length L of 300 nm and the Kuhn length γ −1 of 340 nm are much more probable than other sets of L and γ −1 that equally explain static quantities such as the radius of gyration. The results show that collagen molecules are well characterized by a wormlike chain model.