which region (ribose or base) could be modified to create an inhibitor ?
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which region (ribose or base) could be modified to create an inhibitor ?
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- In centrifugation, after processing all of your protein samples in the laboratory, you are left with one sample to complete. How are you going to resolve the problem safely?What is meant by the description "antiparellel" regarding the two strands that make up DNA?A nonapeptide was treated with dithiothreitol to reduce any disulfide bridges, then partially hydrolyzed, giving rise to the following fragments. What was the sequence of the original polypeptide? Phe-Gln-Asn Pro-Arg-Gly-NH2 Cys-Tyr-Phe Asn-Cys-Pro-Arg Tyr-Phe-Gln-Asn O Cys-Tyr-Phe-GIn-Asn-Cys-Pro-Arg-Gly-NH2 O H2N-Gly-Arg-Pro-Cys-Asn-Gln-Phe-Tyr-Cys O Gly-Arg-Pro-Cys-Tyr-Phe-Gln-Asn-Cys-NH2 Cys-Pro-Arg-Gly-NH2-Cys-Tyr-Phe-Gln-Asn O None of these are correct.
- A researcher creates random copolymers of three nucleotides each by mixing polynucleotide phosphorylase with guanine and adenine nucleotides in a ratio of 5 guanine nucleotides to 1 adenine. Give the different copolymers produced and their theoretical proportions.Consider the image of the attached protein. Now imagine you have a proteolytic enzyme that cleaves peptide-bonds on the C-terminal sides of basic amino acids. If the enzyme cleaves the attached protein, what would the end result be? a.) A single amino acid and a tripeptide b.) two dipeptides Please diagram and explain! Thanks!Can someone give me examples of denatured proteins that can be brought back to native state (renatured)?
- Many antibiotics alter the rate of reaction for enzymes that produce and then cross-link the strands of this polymer together. The image below shows the structure of one antibiotic called penicillin as compared to the portion of the peptidoglycan that undergoes cross linkage. Condon A HS. CH CH CH N-CH cooo Cand cooo wDAla-D-Ala [S] 2. Using the graph above, which condition do you predict was the penicillin condition? 3. Explain how penicillin effects the enzyme. 4. Why it is important to take the full dosage of antibiotics. Briefly explain 5. Is peptidoglycan still being produced in the portion of the graph marked by the circle in condition B?In a gel electropherosis, Glutamate and valine created a double bond. How is that possible?After processing all of your protein samples in the laboratory, you are left with one sample to complete. How are you going to resolve the problem safely?
- You wish to purify a 55 kDa protein, but it is currently present as a mixture with another protein of approximately the same size. Briefly explain a purification strategy that you could use that would enable you to separate the two proteins.Consider the proteins in Figure 1. Assume they are treated with chymotrypsin to cut them into fragments, and then the fragments are separated by gel electrophoresis. What would the fragment patterns look like in the gel for the three different proteins, assuming we can separate polypeptides that differ in size by very small amounts? Complete Figure 2 below to show the location of the uncut polypeptides (- enzyme lanes) and the cut fragments (+ enzyme lanes).Which of the following does not code for an enzyme having both helicase and nuclease activity?a) Rec-Ab) Rec-Bc) Rec-Cd) Rec-D