Question 20 Signal sequences are often found at the C-terminus of the polypeptide chain. True ● False Question 21 Attachment of an isoprenid group to a protein to form a lipid-linked protein Palmitoylation Acetylation Prenylation Lipidation
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- QUESTION NO. 1Targeting a protein to be degraded within proteasomes usually requires ubiquitin. In the function of ubiquitin all of the following are true except: A. ATP is required for activation of ubiquicin. B. a peptide bond forms between the carboxyl terminal of ubiquitin and an ε-amino group of a lysine . C. linkage of a protein to ubiquitin does not always mark it for degradation. D. the N-terminal amino acid is one determinant of selection for degradation. E. ATP is required by the enzyme that transfers the ubiquitin to the protein to be degraded QUESTION NO. 2Much of procollagen formation occurs in the endoplasmic reticulum and Golgi apparatus which requires signal peptide. All of the following statements about targeting a protein for the ER are true except. A. signal peptide usually has a positively charged N-terminus and a stretch of hydrophobic amino acids. B. signal peptide emerging from a free ribosome binds signal recognition…Question 15 Activities found in the rough ER and its functions include the folllowing EXCEPT provides a membrane binding site for the RNA with signal a signal sequence facilitates post-translational modifications allows the entry of polypeptides that will undergo glycosylation provides a membrane scaffold for binding of ribosomes for protein synthesisQuestion:- The enzyme aromatase is found in the cytoplasm of some cells and converts testosterone to estrogen. You decide to test aromatase from a particular cell, and oops, your lab partner admits he drastically increased the pH in all the test tubes. Which of the following is a likely result? a. The enzyme will be denatured and the substrate will not bind to the active site. b. The enzyme will convert testosterone to estrogen at a faster rate. c. The mistake will have no effect on the experiment, because enzymes are not sensitive to pH. d. The free energy will be lowered and the reaction will not proceed spontaneously.
- Question 1Predicting Secondary Structure Which of the following peptides is more likely to take up an -helical structure, and why? (a) LKAENDEAARAMSEA (b) CRAGGFPWDQPGTSNText:QUESTION 16 Protein maturation in the ER includes. A Disulfide bond formation B. proteolytic cleavage C attachment of oligosaccharide d. Prolyl isomertzationQuestion: what is the action of acid and alkali on the enzyme in saliva? Acid: Alkali: (Procedure and data are already given)
- Question 1 options: The specificity pocket of the serine protease chymotrypsin, which interacts with Tyr and Phe-containing peptide sequences, contains a Ser residue. A research group is trying to modify chymotrypsin such that it has a low KM with Trp-containing peptides. Enter the name or abbreviation of an amino acid that the Ser could be mutated to that would likely have the desired effect. (Hint: look at the diagrams of the specificity pockets shown in the course slides, and consider how the Ser would need to change to account for the difference between Tyr/Phe and Trp.)Question 1: Your research project is concerned with the expression and purification of a protein called aldehyde dehydrogenase. Describe in detail all steps required from gene amplification to characterisation of the purified protein.Question: What is the isoelectric point of Cysteine and Glutamate, Illustrate structures and net charges (Determine the isoelectric point based on the pka) please give clear handwritten answer!
- Question: A gene can best be described as a segment of DNA that A. Transcribed B. Is transcribed as well as the associated regulatory regions C. Encoded for a protein or functional RNA D. Encoded for a protein C. Encoded for a protein as well as the associated regulatory regions Choose the Correct with explanationstudent question 1. How do both Hemoglobin and S-adenosylmethionine synthetase form hydrophobic pockets? explain in detail. 2. how does the structure of S-adenosylmethionine synthetase make it resistant to heat denaturation and why, explain in detailQuestion:- For a simple enzymatic reaction that involves only one substrate and follows Michaelis–Menten kinetics, the changes in the concentrations of substrate, product, free enzyme, and the enzyme–substrate complex over the course of the reaction are depicted by solid curves in the graph below. Which curve (1 to 4) corresponds to [ES]? Write down the number as your answer.