Protein is a general term, protein is a branch, and protein is usually a specific protein. For example: chrome protein, hemoglobin, globulin, etc. And protein is the floorboard of all kinds of protein. It can be considered that high-protein foods are rich in protein.

Extended data:

Protein structure type:

Fibrin: A major water-insoluble protein, which usually contains polypeptide chains with the same secondary structure. Many fibrin are closely combined to provide mechanical strength for a single cell or the whole organism, and play a protective or structural role.

Globular proteins: A compact spherical protein containing tightly folded polypeptide chains, many of which are soluble in water. Classical globulin contains pits or cracks that can specifically recognize other compounds.

Keratin: A water-insoluble protein consisting of parallel polypeptide chains in α helix or β folded conformation, which plays a protective or structural role.

Collagen: protein is the most abundant connective tissue in animals, which is composed of procollagen molecules. Procollagen is a kind of protein with right-handed supercoiled structure. Each procollagen molecule is formed by three special left-handed helices (the pitch is 0.95 nm, and each ring contains 3.3 residues).

Companion protein: It forms a complex with the newly synthesized polypeptide chain and helps it to fold correctly into protein with biological functional orientation. Bridesmaid protein can prevent the formation of incorrect folding intermediates and incorrect aggregation of unassembled protein subunits, and assist the transmembrane transport of polypeptide chains and the assembly and disintegration of large multi-subunit proteins.

Myoglobin is a binding protein composed of peptide chain and heme auxiliary group. It is the protein for storing oxygen in muscle, and the curve of oxygen saturation is hyperbolic.

Hemoglobin is a binding protein, which consists of four subunits containing heme auxiliary groups. Hemoglobin is responsible for transporting oxygen from lung to peripheral tissues, and its oxygen saturation curve is S-shaped.

Protein denaturation: The natural conformation of biological macromolecules is destroyed, resulting in the loss of biological activity. Under the action of light, heat, organic solvents and some denaturants, the secondary bond of protein was destroyed, which led to the destruction of the natural conformation of protein and the loss of biological activity.

Renaturation: Under certain conditions, denatured biological macromolecules return to the natural conformation with biological activity.

Allosteric effect: Also known as allosteric effect, it is a phenomenon that the combination of oligomeric protein and ligand changes the conformation of protein, which leads to the change of biological activity of protein.

Baidu Encyclopedia-protein