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Hydroxyproline is a major component of the protein collagen, [3] comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5]
Ann Arbor is a city in and the county seat of Washtenaw County in the U.S. state of Michigan.Founded in 1824 by John Allen and Elisha Rumsey, it was named after the wives of the village's founders, both named Ann, and the stands of bur oak trees they found there.
Proline and its higher homolog pipecolic acid affect the secondary structure of protein. D-alpha-amino acid - L-alpha-amino acid sequence can induce beta hairpin. [1] It suggested that acyclic secondary amino acids are more flexible than cyclic secondary amino acids in protein by replacement of pipecolic acid by N-methyl-L-alanine in efrapeptin C.
Start downloading a Wikipedia database dump file such as an English Wikipedia dump. It is best to use a download manager such as GetRight so you can resume downloading the file even if your computer crashes or is shut down during the download. Download XAMPPLITE from (you must get the 1.5.0 version for it to work). Make sure to pick the file ...
The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase. Other names in common use include Skp1-HyPro GlcNAc-transferase , UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide , GlcNAc-transferase , UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase , and UDP ...
"4-Hydroxyproline, or hydroxyproline (C5H9O3N), is an uncommon amino acid" "Hydroxyproline is a major component of the protein collagen" and under Collagen: "Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals,[1] making up about 25% of the whole-body protein content."
Prolyl 4-hydroxylase subunit alpha-1 is an enzyme that in humans is encoded by the P4HA1 gene. [5] [6]This gene encodes a component of prolyl 4-hydroxylase, a key enzyme in collagen synthesis composed of two identical alpha subunits and two beta subunits.
Two tyrosines separated by a single amino acid, typically valine or another tyrosine, form a short intra-molecular diphenylether crosslink. [11] This can be crosslinked further by the enzyme extensin peroxidase [12] [13] [14] to form an inter-molecular bridge between extensin molecules and thus form networks and sheets.