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How many reducing ends are in a molecule of glycogen that contains 10000 residues with a branch every 10 residues?
The question cannot be answered unambigously based on the information given, since the number depends on how long the chains at each branching point are. If there is one glucose substituent per branching point, the no. of glucose molecules used for the substitution is found by iteration starting by 60000/12 = 5000, but 55000/12 = 4583. Hence the average is where the ends meet: That is about 4791 substituents (depending on how numbers are rounded up or down), which gives 4791 non-reducing ends + 1 from the "backbone = 4792. If there are two glucose substituents per branching point, the no. of branching points, and hence the no. of reducing ends will decrease to about a little less than half of this number because more glucose monomers are "consumed" in the branching chains and the backbone chain will in turn be shorter resulting in fewer possible branching points. However, each branching chain will only have one non-reducing end, and the backbone will stil have only one non-reducing end! :-) Nice question though - I can add that if there is only one large molecule containing all these 60000 glucose monomers there will be only one reducing end no matter how many branching points there are.
What else can I help you with?
The bonds that hold the two chains of an insulin molecule together are?
The bonds that hold the two chains of an insulin molecule together are disulfide bonds. These bonds form between cysteine amino acid residues in the A and B chains of the insulin molecule, creating a stable structure essential for its biological function.
Which amino acid is a thiol?
Cysteine is the amino acid that contains a thiol group (-SH) in its side chain. It can form disulfide bonds with other cysteine residues, contributing to protein structure and stability.
What breaks disulfide bonds in proteins?
Disulfide bonds in proteins are broken by reducing agents, such as dithiothreitol (DTT) or beta-mercaptoethanol. These agents break the sulfur-sulfur bonds in disulfide bonds, leading to the separation of the two cysteine residues involved.
What chemical reaction formed these large molecules?
Large organic molecules (macromolecules) are generally formed by condensation reactions between smaller molecules.Condensation means that a small molecule is formed from the atoms removed during the reaction. In cells, the small molecule is water, so the type of condensation reaction is dehydration.Examples:glucose + (chain of n glucose residues) forms chain of n + 1 residues + wateramino acid + (chain of n amino acid residues) forms chain of n + 1 residues + water
How do the amino acid side chain residues in an helix orient themselves in relation to the center of the helix?
The amino acid side chain residues in an helix orient themselves outward from the center of the helix.
What is the term for the end of the a glycogen branch from which glucose residues are removed during degradation?
Non-reducing end
What is the main enzyme for breaking down glycogen?
The main enzyme for breaking down glycogen is glycogen phosphorylase. This enzyme catalyzes the phosphorylytic cleavage of glucose residues from the glycogen polymer, releasing glucose-1-phosphate for energy production.
What are the carbohydrate that are similar in structure to cellulose?
Cellulose is a biopolymer that is built by beta 1, 6 linkage between the glucose residues. The molecule that resembles it most closely is chitin that has N acetylglucosamine, that is the glucose aminocylated at 2' carbon. In hemicellulose, there is a backbone of glucose and there are side chains of some other glucose residues. Starch and glycogen are also made up of the glucose residues but they are linked by alpha 1-4 linkage.
Tissue in body with highest glycogen content?
Glycogen are found principally in the liver. Glycogen is a polymer of glucose residues linked by α-(1,4)- and α-(1,6)-glycosidic bonds. A second major source of stored glucose is the glycogen of skeletal muscle. , muscle glycogen is not generally available to other tissues, because muscle lacks the enzyme glucose-6-phosphatase.
Protein X contains 10.5lysine residues by weightProtein X has 10 lys residuesWhat is the molwt of protein?
its not determined
What is the difference between the amino acid content of gelatin and casein?
Gelatin is the product of the denaturation of collagen. Collagen is a triple helical molecule that is composed nearly by one third of its residues with Glycine and a 15 to 30% of its residues by Proline and 4-hydroxyproline. When the collagen loses it's triple helix configuration, occurs gelatinization.On the other hand, Casein, the most abundant protein in milk, contains a fairly high number of Proline residues, which do not interact each other, there are no disulfide bridges in it's structure, and therefore it has relatively little tertiary structure.According to above, the main difference between gelatin (denatured collagen) and casein are the 4-hydroxyproline residues, that allow to collagen to form its characteristic triple helix.
What enzyme regulates glycogenolysis?
Actually, three are the enzymes that intervene during glycogen breakdown (glycogenolysis).First, Glycogen phosphorylase (or simply phosphorylase) that catalyzes glycogen phosphorolysis (bond cleavage by the substitution of a phosphate group) to yield glucose-1-phosphate (G1P) releasing only one glucose residue that is at least five residues from a ramification point.The second enzyme is the Glycogen debranching enzymethat removes glycogen's branches, thereby permiting the glycogen phosphorylase reaction (see above) to go to completion. This enzymes also hydrolyzes alpha(1-6)-linked glucosyl units to yield glucose.Finally, Phosphoglucomutase that converts G1P to G6P which is also formed in the first step of glycolysis through the action of either hexokinase or glucokinase.
How does glycogen function in living things?
It is a large, branched polymer of linked glucose residues (portions of larger molecules) that can be readily mobilized as an energy source, increasing the amount of glucose immediately available to the organism between meals and during muscular activity.
How does glycogen function living things?
It is a large, branched polymer of linked glucose residues (portions of larger molecules) that can be readily mobilized as an energy source, increasing the amount of glucose immediately available to the organism between meals and during muscular activity.
How many amino acid residues are in an insulin molecule?
Human insulin (I'm not sure about other species) is a 51-residue peptide. It's stored as a hexamer, but the active form is the monomer.
The bonds that hold the two chains of an insulin molecule together are?
The bonds that hold the two chains of an insulin molecule together are disulfide bonds. These bonds form between cysteine amino acid residues in the A and B chains of the insulin molecule, creating a stable structure essential for its biological function.
What functional groups are found in insulin?
Insulin contains a peptide functional group due to its protein structure. Additionally, it contains amino acid residues that contribute to its biological activity and role in controlling blood sugar levels.
