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Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage. Type II collagen is organised into fibrils. This fibrillar network of collagen ...
Swiss-model. Domains. InterPro. Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates. Type I forms large, eosinophilic fibers known as collagen fibers, which make up most of the rope ...
A representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red). Proteins are large biomolecules and ...
Protein efficiency ratio. Protein efficiency ratio (PER) is based on the weight gain of a test subject divided by its intake of a particular food protein during the test period. From 1919 until very recently [when?], the PER had been a widely used method for evaluating the quality of protein in food.
Ionization and Brønsted character of N-terminal amino, C-terminal carboxylate, and side chains of amino acid residues The common natural forms of amino acids have a zwitterionic structure, with −NH + 3 (−NH + 2 − in the case of proline) and −CO − 2 functional groups attached to the same C atom, and are thus α-amino acids, and are the only ones found in proteins during translation ...
Vitamin B12, also known as cobalamin, is a water-soluble vitamin involved in metabolism.[2] It is one of eight B vitamins. It is required by animals, which use it as a cofactor in DNA synthesis, and in both fatty acid and amino acid metabolism.[3] It is important in the normal functioning of the nervous system via its role in the synthesis of ...
Infectious diseases. A prion / ˈpriːɒn / ⓘ is a misfolded protein that can induce misfolding of normal variants of the same protein and trigger cellular death. Prions cause prion diseases known as transmissible spongiform encephalopathies (TSEs) that are transmissible, fatal neurodegenerative diseases in humans and animals.