F. Briki et al., Organization of microfibrils in keratin fibers studied by X-ray scattering- Modelling using the paracrystal concept, BBA-PROT ST, 1429(1), 1998, pp. 57-68
Citations number
18
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
Low-angle X-ray scattering patterns of hard alpha-keratin fibers have been
studied for more than 50 years but a completely convincing modelling has ne
ver been presented. The models which have been proposed so far are specific
to the sample and cannot be adapted to others, mainly because they do not
use a parametric analytical expression of the distribution function describ
ing the relative positions of the microfibrils. Our new approach is based o
n a paracrystal distribution function. In addition, a huge background origi
nating from a non-ordered matrix is taken into account. Various hard alpha-
keratins from different origins have been studied using our approach. From
the rather good modellings obtained, it appears that the diameter of the mi
crofibril is not origin dependent (7.4 nm) whereas the distances between mi
crofibrils and their electron density profiles are. Hair microfibrils can b
e reasonably approximated by a solid cylinder but a core and an outer ring
are necessary for porcupine. Our method is of course not limited to keratin
microfibrils; it can be used for modelling equatorial X-ray scattering pro
files of all types of hexagonal fibrillar assemblies, which are in fact wid
ely found in biological tissues. (C) 1998 Elsevier Science B.V. All rights
reserved.