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A synchondrosis (or primary cartilaginous joint) is a type of cartilaginous joint where hyaline cartilage completely joins together two bones. [1] Synchondroses are different from symphyses (secondary cartilaginous joints), which are formed of fibrocartilage, and from synostosis (ossified junctions), which is the fusion of two or more bones.
At the top level are all alpha proteins (domains consisting of alpha helices), all beta proteins (domains consisting of beta sheets), and mixed alpha helix/beta sheet proteins. While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred to as metamorphic proteins. [5]
A symphysis (/ ˈ s ɪ m. f ɪ. s ɪ s /, pl.: symphyses [1]) is a fibrocartilaginous fusion between two bones. It is a type of cartilaginous joint, specifically a secondary cartilaginous joint. A symphysis is an amphiarthrosis, a slightly movable joint. A growing together of parts or structures. Unlike synchondroses, symphyses are permanent. [2]
Protein domains. The two shown protein structures share a common domain (maroon), the PH domain, which is involved in phosphatidylinositol (3,4,5)-trisphosphate binding. Proteins are frequently described as consisting of several structural units. These units include domains, motifs, and folds.
The words protein, polypeptide, and peptide are a little ambiguous and can overlap in meaning. Protein is generally used to refer to the complete biological molecule in a stable conformation, whereas peptide is generally reserved for a short amino acid oligomers often lacking a stable 3D structure. But the boundary between the two is not well ...
The first two steps of the urea cycle take place within the mitochondrial matrix of liver and kidney cells. In the first step ammonia is converted into carbamoyl phosphate through the investment of two ATP molecules. This step is facilitated by carbamoyl phosphate synthetase I.
Fibrous proteins are structural or storage proteins that are typically inert and water-insoluble. A fibrous protein occurs as an aggregate due to hydrophobic side chains that protrude from the molecule. A fibrous protein's peptide sequence often has limited residues with repeats; these can form unusual secondary structures, such as a collagen ...
The colloidal protein hypothesis stated that proteins were colloidal assemblies of smaller molecules. This hypothesis was disproved in the 1920s by ultracentrifugation measurements by Theodor Svedberg that showed that proteins had a well-defined, reproducible molecular weight and by electrophoretic measurements by Arne Tiselius that indicated ...