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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.
Arabinogalactan-proteins (AGPs) are highly glycosylated proteins (glycoproteins) found in the cell walls of plants. Each one consists of a protein with sugar molecules attached (which can account for more than 90% of the total mass). They are members of the wider class of hydroxyproline (Hyp)-rich cell wall glycoproteins, a large and diverse ...
Extensins are a family of flexuous, rodlike, hydroxyproline-rich glycoproteins (HRGPs) of the plant cell wall. [1] [2] They are highly abundant proteins. There are around 20 extensins in Arabidopsis thaliana. They form crosslinked networks in the young cell wall.
N-linked protein glycosylation (N-glycosylation of N-glycans) at Asn residues (Asn-x-Ser/Thr motifs) in glycoproteins. [1] Glycoproteins are proteins which contain oligosaccharide (sugar) chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification.
Chlamydomonas reinhardtii is a single-cell green alga about 10 micrometres in diameter that swims with two flagella.It has a cell wall made of hydroxyproline-rich glycoproteins, a large cup-shaped chloroplast, a large pyrenoid, and an eyespot apparatus that senses light.
3273 94175 Ensembl ENSG00000113905 ENSMUSG00000022877 UniProt P04196 Q9ESB3 RefSeq (mRNA) NM_000412 NM_053176 RefSeq (protein) NP_000403 NP_444406 Location (UCSC) Chr 3: 186.66 – 186.68 Mb Chr 16: 22.77 – 22.78 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Histidine-rich glycoprotein (HRG) is a glycoprotein that in humans is encoded by the HRG gene. The HRG protein is produced ...
Lysine. Technically, any organic compound with an amine (–NH 2) and a carboxylic acid (–COOH) functional group is an amino acid. The proteinogenic amino acids are a small subset of this group that possess a central carbon atom (α- or 2-) bearing an amino group, a carboxyl group, a side chain and an α-hydrogen levo conformation, with the exception of glycine, which is achiral, and proline ...
E.g., DNA-binding proteins have their active regions rich with arginine and lysine. The strong charge makes these two amino acids prone to be located on the outer hydrophilic surfaces of the proteins; when they are found inside, they are usually paired with a corresponding negatively charged amino acid, e.g., aspartate or glutamate. Leucine: L Leu