Identify the true statements regarding disulfide bridges (disulfide bonds). disulfide bridges have a stabilizing effect on proteins. disulfide bridges are formed by an irreversible oxidation reaction. disulfide bridges can exist between two amino acid residues on different chains. a disulfide bridge forms between two cysteine residues. disulfide bridges are important to primary and secondary structure.
Option (1), (2), and (4). Explanation: A disulphide bond is also known by the name disulphide bridge. This is a type of a covalent bond by the oxidation of the sulfhydryl groups. This bond is important for the folding of proteins. Disulfide bonds is important for the stabilization of protein. Their main effect is to stabilize and the proper functioning of protein. The disulfide bond is present between the two amino acids of the different polypeptide chain. The amino acids that contain cysteine residues has the ability to form this bond. Thus, the correct answer is option (1), (2), and (4).
The answer is 1,3,4 Explanation: I got it right on the homework
(A) Branching increases glycogen solubility. (B) New α‑1,6 linkages can only form if the branch has a free reducing end. (C) The number of sites for enzyme action on a glycogen molecule is increased through α‑1,6 linkages. E) The reaction that forms α‑1,6 linkages is catalyzed by a branching enzym
(E) Explanation: The binding of glucose to liver phosphorylase a shifts the equilibrium from the active form to the inactive form.
a. New alpha- 1,6 linkages can only form if the branch has a free reducing end b. The number of sites for enzyme action on a glycogen molecule is increased through alpha- 1,6 linkages c. At least four glucose residues separate alpha-1,6 linkages e. The reaction that forms alpha-1,6 linkages is catalyzed by a branching enzyme. Explanation: Glycogen i is the main storage polysaccharide in animals. It a homoplymer of (alpha-1–>4)-linked subunits of glucose molecules, with alpha-1—>6)-linked branches. The alpha-1,6 branches are formed by the glycogen-branching enzyme which catalyzes the transfer of about 7 glucose residues from the non-reducing end of a glycogen branch having at least 11 residues to the C-6 hydroxyl group of a glucose residue which lies inside the same glycogen chain or another glycogen chain, thereby forming a new branch. This ensures that there are at least four glucose residues separating alpha-1,6 linkages. The effect of branching is that it makes the glycogen molecule more soluble and also increases the number of non-reducing ends, thereby increasing the number of sites for the action of the enzymes glycogen phosphorylase and glycogen synthase.
At least four glucose residues separate α‑1,6 linkages. The number of sites for enzyme action on a glycogen molecule is increased through α‑1,6 linkages. The reaction that forms α-1,6 linkages is catalyzed by a branching enzyme. Explanation: Glycogen is a polymer of glucose and is the primary carbohydrate storage form in animals. The polymer is composed of glucose units linked in alpha(1-4) straight chains and alpha(1-6) branches which occur on average every 8-12 straight chain glucose residues. It has a reducing and non-reducing end. The end of the molecule containing a free carbon number one on glucose is called a reducing end. The other ends are all called non-reducing ends. During the breakdown of glycogen, glucose units are removed one at a time from the non-reducing end until a point about four glucose residues away from a branch which will require a debranching enzyme to act for further breakdown to occur. Since many such branches occur in a glycogen molecule, it makes it possible for breakdown of glycogen to occur at many points speedily. Glycogen branching enzyme is required to make alpha (1-6) glycosidic bonds. It transfers 6 to 7 glucose units from the non-reducing end of a straight chain glycogen molecule to an interior position of the same or another glycogen molecule forming alpha (1-6) bonds.
C. The reaction that forms α-1, 6 linkages is catalyzed by branching enzymes. Explanation: α-glucan branching enzyme which can also be called the Brancher enzyme or glycogen-branching enzyme is the enzyme responsible for the side chain reaction that attaches at carbon atom 6 of a glucose unit (an α-1,6-glycosidic bond). This branching enzyme attaches a string of seven glucose units to the carbon at the C-6 position on the glucose unit, forming the α-1,6-glycosidic bond.
The globin chains of myoglobin and hemoglobin prevent the oxidation of Fe2 to Fe3 , which irreversibly binds oxygen. The cooperativity of oxygen binding in hemoglobin arises from electronic interactions between heme groups.
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