In my biochemistry course, we are completing a project where we take the human insulin degrading enzyme (IDE) and make a mutation, propose what would happen upon said mutation, and determine methods for testing this in the lab. The
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Q: What is point mutation.give one example?
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Q: Point mutations arise more commonly than other types of mutations. -True or False
A: Point mutation is a mutation in which one base pair in the DNA sequence get altered.
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Q: In order to manufacture insulin for patients with diabetes, scientists create recombinant DNA by…
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Q: _____ Mutants Are Useful in ______ the Order in Which Proteins Function.
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Q: a. Identify the type of mutation shown below. b. How many amino acids are affected? c. What type of…
A: Ans a. The type of mutation shown below is point mutaion. A point mutation or replacement is a…
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Q: What would happen if an allosteric enzyme had a T/R ratio of 0 as a consequence of a mutation?
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Q: loss of function mutation
A: Sorry for the inconvenience. As per bartleby guidelines we should not give the answers for 2…
Q: When the amino acid sequences of insulin isolated from different organisms were determined,…
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Q: Why is recombinant Insulin produced by genetic engineering need to be processed?
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Q: cause mutation
A: Introduction :- A mutation is a change that occurs in DNA sequence, either due to mistakes when the…
Q: Determine the effect of the following mutations on the DNA sequence. In each case, the mutation is…
A: Any detectable, inheritable qualitative or quantitative change in genetic material of an organism…
Q: Determine the effect of the following mutations on the DNA sequence. In each case, the mutation is…
A: The mutation is a molecular process that alter the nucleotide sequence of the DNA. As the mRNA is…
Q: Describe the consequences of frame shift mutation.
A: The mutation in which insertion or deletion of the nucleotide takes place is called frameshift…
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- Allosteric Regulation of Ribonucleotide Reductase by ATP and Deoxynucleotides Describe the underlying rationale for the regulatory effects exerted on ribonucleotide reductase by ATP, dATP, dTTP, and dGTP.Why is derivatization (i.e., transesterification) of triglycerides or lipids to fatty acid methyl esters needed for the GC/MS experiment?At body temperature, L-aspartate in proteins race-mizes to D-aspartate at an appreciable rate. Most pro-teins in the body have a very low level of D-aspartate, if itcan be detected at all. Elastin, however, has a fairly highlevel of D-aspartate. Moreover, the amount of D-aspartateincreases in direct proportion to the age of the person fromwhom the sample was taken. Why do you suppose thatmost proteins have little if any D-aspartate, while elastinhas levels of D-aspartate that increase steadily with age?
- In the fungus Neurospora, some mutants were obtainedthat lacked activity for a certain enzyme. The mutationswere found, by mapping, to be in either of two unlinkedgenes. Provide a possible explanation in reference to quaternary protein structureWe learned that three different amino acid transformations of PLP-dependent enzymes canresult from different conformations of the PLP-amino acid imine adduct in the active site.Starting from the PLP adduct of (S)-serine, show mechanisms fora) Decarboxylation of serineb) Racemization of serinec) Conversion of serine to glycine and formaldehyde.Thesecondarystructureofaproteinisinfluencedbybothhydrogen bonding and London dispersion forces. a. Usingastructuralformula,showanexampleofhydrogenbonding between the serine portion of a protein and the tyrosine portion b. Usingastructuralformula,showanexampleofLondondispersionforces between the leucine portion of a protein and the valine portion
- What does this important observation imply about the relation between the amino acid sequence of insulin and its three-dimensional structure?n a particular enzyme, an alanine residue is located in a cleft where the substrate binds. A mutation that changes this residue to glycine has little effect on activity; however, another mutation, which changes the alanine to a glutamate residue, leads to a complete loss of activity. Provide a brief explanation for these observation. In Figure 6-11,a. in view of the position of HPA oxidase earlier in thepathway compared to that of HA oxidase, would youexpect people with tyrosinosis to show symptoms ofalkaptonuria?b. if a double mutant could be found, would you expecttyrosinosis to be epistatic to alkaptonuria?
- What would be the metabolic consequences and symptoms of having a mutated form of phosphofructokinase-1 in muscle that is no longer allosterically regulated by [H+]? Speculate on how a patient with this mutation could deal with this.The interconverison of DHAP and GAP greatly favors the formation of DHAP at equilibirum. Yet the conversion of DHAP by triose phosphate isomerase proceeds readily. Why?Insulin possesses two polypeptide chains denoted A and B that are linked by disulfide bonds. Upon denaturation by reduction of the SH groups of insulin, followed by reoxidation, only 7% of the hormone activity is recovered. This is the level of activity expected for random pairing of cysteine residues to form disulfide bonds. How can these data be reconciled with the hypothesis that the amino acid sequence directs protein folding?