3. Why glycogen in muscle cells cannot be stained blue-black by iodine solution?
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- 9. If a commercially available insulin preparation contains 1 ppm of pro-insulin, how many micrograms of proinsulin would be contained in a 10-mL vial of insulin?13. What value do N-linked saccharides serve for membrane surface proteins? Which amino acid residue(s) do we find involved in N-linked bonds?1.One of the main sources of sphingosine in the body is in the cell membrane. What complication could arise from the biological synthesis of ceramide?
- 10. What are alkaloidal reagents so called? What is the effect of alkaloidal reagents on proteins? Why are proteins affected by alkaloidal reagents? Why is picric acid used in the treatment of burns?24. Addition and removal of what type of chemical group is frequently used in cell signaling events, including those that regulate the cell cycle? Methyl group Phosphate group Amino group Carboxylate group2. A functional protein that is approximately 110 kDa in size has all its cysteine residues joined with disulfide bonds. It has one cysteine residue per 100 amino acids. When heated at 85°C it lost activity, but when it was allowed to cool, the activity was restored? Please answer the following questions: a) How many disulfide bonds the protein has? Show how you came up with the answer. b) What is the molecular basis for the protein behavior in restoring activity?
- 1. Theoretically, a protein could assume a virtually infinite number of configurations and conformations. Suggestseveral features of proteins that drastically limit the actual number. 2. What are the greatest structural features that differentiate sphingolipids from phosphoglycerides? 3. High levels of glucose-6-phosphate inhibit glycolysis. If the concentration of glucose-6-phosphate decreases,activity is restored. Why?4. What four main molecular components make up a phospholipid like phosphatidylcholine? (Note: if there are two of one component, it counts as one!)4. Which amino acids do not react to produce a purple color with ninhydrin. Why?