N-terminal analysis
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- select the correct option molecular chaperone protein function by a.Mediating disulfide bond formation d.Enhancing salt bridge formationynthesizing new protein when one is folded c.Preventing premature folding by binding hydrophobic regions of protein d.Synthesizing new protein when one is folded e. none of the optionSuppose you have a cell-lysis sample containing genomic DNA, a complex mixture of proteins, and debris. Describe different commonly used analytical methods to i) analyze the molecular masses of the protein mixture. ii) detect the composition (what specific amino acids are there in what proportion) of a specific protein from the mixture. iii) deduce the sequence of some particular proteins from the mixture contentWhen a protein is denatured using heat Select one: a. its C-terminal will change. b. its tertiary structure will change. c. its amino acid sequence will change. d. its amino acid composition will change.
- Nitrous acid replaces amino groups with keto groups, a processcalleda. alkylation.b. deamination.c. depurination.d. crosslinking.Define the following terms: a. cap-binding complex b. 43S preinitiation complex c. poly(A)-binding protein d. 48S initiation complex e. glycosylationWhich of the following about protein denaturation is not trueA. It is always irreversible B. It is a shape change C. It may be due to pH / temperature change D. Most of the proteins denature when transferred from aqueous environment to organs solvents E. Its function is lost.
- Which of the following does not describe protein modifications? please explain the answer a.They can promote multiprotein complex formation b.They can target a protein for proper localization c.They can regulate protein stability d.They are always permanent changesElectrophoresis is a method used to sort proteins by their size. Why is a detergent added to the buffer? a) Because SDS forms micelles in which the proteins can be transported through the gel in b) Because SDS lowers the pH of the buffer c) Because SDS denaturs the protein d) Because smaller proteins move more slowly through the gel thenWhy are protein samples denatured before running SDS PAGE?A. To allow separation based on chargedB. To be able to visualize the proteinC. To allow separation based on sizeD. To be able to load samples correctly on the SDS-PAGE gel
- The rate of migration of a protein through an SDS-poly-acrylamide gel is NOT influenced by A. Strength of the electric field B. Size of the protein. C. Pore size of the gel. D. Charge of the protein.RNAses can be found a) In cells b) Countertops c) On hands d) Everywhere The ratio of absorption at 260nm to absorption at 280nm is commonly used to assess a) The concentration of DNA and RNA. b) The purity of protein. c) Whether your DNA or RNA is contaminated Trizol. d) The concentration of protein in your sample.The growing peptide extends out of a tunnel located above the ... A) A site B) P Site C) F site D) E site