Modeling the lateral organization of collagen molecules in fibrils using the paracrystal concept.

Abstract:

:A characteristic feature of the dense phases formed by fiber-shaped molecules is their organization into parallel rods packed in a hexagonal or pseudo-hexagonal lateral network. This is typically the case for the collagen triple helices inside fibrils, as confirmed by recent X-ray diffraction experiments carried out on highly crystallized fibers obtained by immersing the freshly extracted fibers in a salt-controlled medium. However such diffraction patterns also generally exhibit additional features in the form of diffuse scattering, which is a clear signature of a low degree of lateral ordering. Only few studies have analyzed and modeled the lateral packing of collagen triple helices when the structure is disordered. Some authors have used the concept of short-range order but this approach does not contain any echo of a hexagonal order. In this study, we use an analytical expression derived from the paracrystal model which retains the hexagonal symmetry information and leads to a good agreement with the experimental data in the medium-angle region. This method is quite sensitive to the degree of disorder and to the inter-object distance. One clear result is that the shift in peak positions, generally attributed to variations in intermolecular distances, can also arise from a change in the degree of ordering without any significant modification of the distances. This underlines the importance of evaluating the degree of ordering before attributing a shift in peak position to a change in the unit-cell. This method is generic and can be applied to any system composed of rod-shaped molecules.

journal_name

J Struct Biol

authors

Doucet J,Briki F,Gourrier A,Pichon C,Gumez L,Bensamoun S,Sadoc JF

doi

10.1016/j.jsb.2010.11.018

subject

Has Abstract

pub_date

2011-02-01 00:00:00

pages

197-201

issue

2

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(10)00355-2

journal_volume

173

pub_type

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