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Hydroxyproline is found in few proteins other than collagen. For this reason, hydroxyproline content has been used as an indicator to determine collagen and/or gelatin amount. However, the mammalian proteins elastin and argonaute 2 have collagen-like domains in which hydroxyproline is formed.
The bacterial DNA is not packaged using histones to form chromatin as in eukaryotes but instead exists as a highly compact supercoiled structure, the precise nature of which remains unclear. [6] Most bacterial chromosomes are circular, although some examples of linear chromosomes exist (e.g. Borrelia burgdorferi). Usually, a single bacterial ...
Procollagen-proline dioxygenase, commonly known as prolyl hydroxylase, is a member of the class of enzymes known as alpha-ketoglutarate-dependent hydroxylases.These enzymes catalyze the incorporation of oxygen into organic substrates through a mechanism that requires alpha-Ketoglutaric acid, Fe 2+, and ascorbate.
Because of the many functions they have, changes in O-glycosylation are important in many diseases including cancer, diabetes and Alzheimer's. O-glycosylation occurs in all domains of life, including eukaryotes, archaea and a number of pathogenic bacteria including Burkholderia cenocepacia, [3] Neisseria gonorrhoeae [4] and Acinetobacter ...
The chemical structure of hydroxyproline (4-hydroxypyrrolidine- 2-carboxylic acid). Date: 1 May 2007: Source: Self-made in bkchem; edited in vim. Author: User:Mysid ...
In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.
The cyclic structure of proline's side chain locks the angle φ at approximately −65°. [19] Proline acts as a structural disruptor in the middle of regular secondary structure elements such as alpha helices and beta sheets; however, proline is commonly found as the first residue of an alpha helix and also in the edge strands of beta sheets.
Cleavage of the proline- and hydroxyproline-rich proteins of the Chlamydomonas cell wall; also cleaves azocasein, gelatin and Leu-Trp-Met-Arg-Phe-Ala. This glycoprotein is present in Chlamydomonas reinhardtii gametes. Gram-positive bacteria regulate autolysins with teichoic acid molecules attached to the tetrapeptide of the peptidoglycan matrix.