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HXFC
HX Quality Life
The most abundant proteins in the extracellular matrix are members of the collagen family. Collagens were once considered to be a group of proteins with a characteristic molecular structure with their fibrillar structures contributing to the extracellular scaffolding. Thus, collagens are the major structural element of all connective tissues and are also found in the interstitial tissue of virtually all parenchymal organs, where they contribute to the stability of tissues and organs and maintain their structural integrity.
A structural prerequisite for the assembly into a triple helix is a glycine residue, the smallest amino acid, in every third position of the polypeptide chains resulting in a (Gly-X-Y)n repeat structure which characterizes the 'collagenous' domains of all collagens.The X and Y position is often occupied by proline and hydroxyproline.
Thus, the C-propeptide is thought to play a fundamental role in the initiation of triple helix formation, whereas the N-propeptide is thought to be involved in the regulation of primary fibril diameters
The short non-helical telopeptides of the processed collagen monomers are involved in the covalent cross-linking of the collagen molecules as well as linking to other molecular structures of the surrounding matrix.
Collagen can be added to bread to prolong the aging time of bread, improve the volume and softness of bread. Gelatin has the function of absorbing water and supporting the skeleton. Its particles can be interwoven into a network structure after being dissolved in water; After condensation, sugar and water can be filled to keep the soft candy in a stable shape, bear a large load without deformation, and improve the nutritional value of the candy, so that low-calorie candy can be developed.
The most abundant proteins in the extracellular matrix are members of the collagen family. Collagens were once considered to be a group of proteins with a characteristic molecular structure with their fibrillar structures contributing to the extracellular scaffolding. Thus, collagens are the major structural element of all connective tissues and are also found in the interstitial tissue of virtually all parenchymal organs, where they contribute to the stability of tissues and organs and maintain their structural integrity.
A structural prerequisite for the assembly into a triple helix is a glycine residue, the smallest amino acid, in every third position of the polypeptide chains resulting in a (Gly-X-Y)n repeat structure which characterizes the 'collagenous' domains of all collagens.The X and Y position is often occupied by proline and hydroxyproline.
Thus, the C-propeptide is thought to play a fundamental role in the initiation of triple helix formation, whereas the N-propeptide is thought to be involved in the regulation of primary fibril diameters
The short non-helical telopeptides of the processed collagen monomers are involved in the covalent cross-linking of the collagen molecules as well as linking to other molecular structures of the surrounding matrix.
Collagen can be added to bread to prolong the aging time of bread, improve the volume and softness of bread. Gelatin has the function of absorbing water and supporting the skeleton. Its particles can be interwoven into a network structure after being dissolved in water; After condensation, sugar and water can be filled to keep the soft candy in a stable shape, bear a large load without deformation, and improve the nutritional value of the candy, so that low-calorie candy can be developed.
