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pro vyhledávání: '"T. J. Wess"'
Autor:
T J, Wess
Publikováno v:
Advances in protein chemistry. 70
The majority of collagen in the extracellular matrix is found in a fibrillar form, with long slender filaments each displaying a characteristic approximately 67?nm D-repeat. Here they provide the stiff resilient part of many tissues, where the inhere
Publikováno v:
Journal of muscle research and cell motility. 23(5-6)
Fibrillin-rich microfibrils are evolutionarily ancient macromolecular assemblies of the extracellular matrix. They have unique extensible properties that endow vascular and other tissues with long-range elasticity. Microfibril extensibility supports
Publikováno v:
Mechanics of Elastic Biomolecules ISBN: 9789401039710
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e509207dc58f5e008c2dad2a5d3acf3d
https://doi.org/10.1007/978-94-010-0147-2_17
https://doi.org/10.1007/978-94-010-0147-2_17
Publikováno v:
Journal of molecular biology. 275(2)
X-ray diffraction of rat tail tendon shows that type I collagen fibrils contain regions of three-dimensional crystalline arrays; where molecular packing is speculated to be by a staggered sheet or microfibril arrangement. The X-ray diffraction patter
Publikováno v:
Basic life sciences. 64
The chemical reactivity of collagen can be studied using neutron diffraction (a non-destructive technique), for certain reaction types. Collagen contains a number of lysine and hydroxylysine side chains that can react with aldehydes and ketones, or t
Publikováno v:
Alcohol and alcoholism (Oxford, Oxfordshire). 29(4)
The location of acetaldehyde binding sites in the axial unit cell of tendon collagen was investigated by neutron diffraction. Acetaldehyde forms spontaneous cross-links with specific residues in collagen. The use of deuterated acetaldehyde increased