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Fibrillar collagens triple helix

In addition to the hydrogen bonding which stabilises the triple helix, a variety of links are formed between adjacent molecules within the fibrillar structure. In particular, covalent bonds are formed between the ends of one collagen macromolecule in what is termed the telopeptide region and the helical structure of an adjacent one. [Pg.97]

X 1060) (collagen), skin, bone, tendon. Three-stranded triple helix. The most abundant protein in animals. Fibrillar... [Pg.3]

Fibrillar proteins have a specific secondary structure. For example, the basic secondary structure of keratin consists of two pairs of closely linked right-handed a-hehces (a superhehx) that are coiled into a left-handed hehx. The basic secondary structure of collagen is a triple hehx in which the left-handed polypeptide helix is coiled into the right-handed superhehx. [Pg.50]

See other pages where Fibrillar collagens triple helix is mentioned: [Pg.508]    [Pg.307]    [Pg.341]    [Pg.184]    [Pg.97]    [Pg.238]    [Pg.575]    [Pg.142]    [Pg.472]    [Pg.501]    [Pg.275]    [Pg.13]    [Pg.433]    [Pg.343]    [Pg.386]    [Pg.48]    [Pg.266]    [Pg.433]    [Pg.50]    [Pg.55]    [Pg.56]    [Pg.103]    [Pg.151]    [Pg.218]    [Pg.908]    [Pg.296]    [Pg.296]    [Pg.297]    [Pg.299]    [Pg.299]    [Pg.35]    [Pg.274]    [Pg.503]    [Pg.180]    [Pg.295]    [Pg.49]    [Pg.66]    [Pg.14]   
See also in sourсe #XX -- [ Pg.46 , Pg.49 ]



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