acid Changing a hydrophobic amino acid in the cofactor pocket to a positively ch
ID: 257979 • Letter: A
Question
acid Changing a hydrophobic amino acid in the cofactor pocket to a positively charged amino will allow this en d. zyme to now prefer NADP rather than NAD 28 With respect to beta-galactosidase activity, which of the following statements is true . Beta-galactosidase is much smaller than most other hydrolytic enzymes b. It may be possible to engineer a smaller version of Beta-galactosidase that sti c. From an industrial viewpoint, it would be far better to manufacture a larger versiono ll functions galactosidase All of these statements are true. d. 29. Directed evolution is a technique used to later the function of enzymes of the following approaches are used in directed evolution. without needing structural data. Which a Different domains of various proteins can be recombined together to create new enzymes b. Target mutagenesi s of the putative active site can be carried out to alter enzyme function. e can be mutated using error-prone PCR and then new enzymes functions selected d. All of the above are appropriate approaches e. Some of the above are appropriate approaches 30. The steps involved in engineering new proteins that contain non-natural amino acids include ning and directed evolution of a gene for tRNA synthetase to create the new tRNA charged with the non-natural amino acid Engineering genes for the new tRNA so it will bind to the amber codon. Cloning all of these evolved genes into Methanococcus jannaschii All of the above. a. Clo c. d. e. Some of the above 31. Recombinant human erythropoietin linked Glycosylation sites. This resulted in is now on the market. When this protein was engineered, it had extra N- a. A decrease in the affinity of erythropoietin for its receptor b. The half-life of the engineered protein was longer. c. Overall, d. All of the above. e. Some of the above. l the engineered protein had increased clinical activity 32. When the DNA binding domain of Fokl is combined with the recognition domain of the Gal4 activator, the result is a. A recombinant protein with Zinc finger binding b. A restriction enzyme that cuts right in the middle of the Gal4 DNA recognition sequence. c. A nuclease that recognizes the GAL4 DNA recognition sequence and cuts next to it. d. An endonuclease that cuts nonspecifically 33.Zinc finger domains are found in many regulatory proteins. OF the following properties, which is not a property of a zinc finger domain? a. Consists of 25-30 amino acids arranged around a Zinc ion b. Binding to cysteines and histidines holds the zinc ion in place. c. Each domain has nuclease activity d. One Zinc finger motif binds 3 base pairs 34. DNA shuffling is a method of artificial evolution of new enzyme activities. Which of the following steps may not be needed? a. Mutating the gene and obtaining a mutant bank. b. Digesting to obtain different pieces of DNA C. Reassembling the pieces of DNA, generating novel combinations. d. Screening the new combinations for activityExplanation / Answer
28. a. Beta galactosidase enzyme has 120Da, 1024 amino acids only where as other hydrolytic enzymes are much larger.
29. d. all of them are correct approaches.
30. d. All of the above are correct.
31. c. Overall the engineered protein had increased clinical activity. Because it may have an impact on the structure, solubility antigenicity, folding and its stability.
32. a. A recombinant protein with zinc finger binding because zinc finger domain also been joined to the nuclease domain of Fokl. The zinc finger is a common DNA binding motif found in many regulatory proteins.
33. c.Each domain has nuclease activity.
34.a. Mutating the gene and obtaining a mutant bank.
Related Questions
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.