Brown, A. (2013). Double twist liquid crystal model of collagen structure. Perimeter Institute for Theoretical Physics. https://pirsa.org/13120023
MLA
Brown, Aidan. Double twist liquid crystal model of collagen structure. Perimeter Institute for Theoretical Physics, Dec. 05, 2013, https://pirsa.org/13120023
BibTex
@misc{ scivideos_PIRSA:13120023,
doi = {10.48660/13120023},
url = {https://pirsa.org/13120023},
author = {Brown, Aidan},
keywords = {},
language = {en},
title = {Double twist liquid crystal model of collagen structure},
publisher = {Perimeter Institute for Theoretical Physics},
year = {2013},
month = {dec},
note = {PIRSA:13120023 see, \url{https://scivideos.org/pirsa/13120023}}
}
Collagen is the main component of connective tissue and the most abundant protein in mammals. The structure of collagen is hierarchical with the triple-helical molecules organizing into fibrils and fibrils contained in higher-order arrangements. A fibril may be considered as a liquid crystal of individual triple helices. Their chiral molecular structure can lead to a macroscopic helical arrangement known as the cholesteric phase which has been observed in fragments of collagen fibrils. The cholesteric orientation can vary with radial distance in the fibril as a double twist. We numerically minimize mean-field Frank free energy in the bulk to solve for the liquid crystal orientation as a function of radial distance (r). By also considering surface terms the overall energy per fibril area is minimized to find the optimal fibril radius R and molecule orientation on the fibril surface (R) both of which may be compared to experimental measurements.
