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It should be noted that, within the strained micronetwork, there must be some fibrils which do not carry significant tensile load.
These inclusions contain some fibrils, which are probably muscular.
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The sheaths of some of them contain cellulose-like homoglucan fibrils which are cross-linked by minor monosaccharides.
TEM did not reveal any obvious differences in fibril density between Aβ incubated under oxidizing and non-oxidizing conditions, although the oxidized sample appears to show shorter, more self-associated fibrils, which may be consistent with some interfibrillar crosslinking.
Some cuts of meat including poultry expose the microscopic regular structure of intracellular muscle fibrils which can diffract light and produce iridescent colours, an optical phenomenon sometimes called structural colouration.
Only later and gradually, however, the spheres stick together, forming tiny rods filaments and much larger fibrils, which in turn accumulate into insoluble deposits of protein called amyloid plaque.
The outermost layer is a fine network of fibrils, which, at the ends of the muscle, extend into the tendons and form the structural link with them.
In contrast, the widely distributed fibrillar collagens I and III, form covalently bonded fibrils which resist tensile forces [22 24].
This may have occurred because of its activity on the collagen fibrils, which can protect them from degradation.
One peptide (PTP-7c) formed stable amyloid fibrils, which did not completely dissolve under acidic conditions.
Radial arrays of dense type I collagen fibrils, which account for 90% of the organic matrix, and noncollagenous acidic proteins play an important role in calcification [5].
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