What biological rationale can explain why there are so few variants observed at position 65 of the heme distal ligand and position 94 of the heme proximal ligand of myoglobin? Why does the number of variants differ between the two sites?
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Question:-
What biological rationale can explain why there are so few variants observed at position 65 of the heme distal ligand and position 94 of the heme proximal ligand of myoglobin? Why does the number of variants differ between the two sites?
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- THOUGHT QUESTION Imagine we identify a gene that is directly responsible for the effects of vasopressin on male mammals, including humans-we will call it trust1-that leads to the production of a vasopressin receptor in the brain, which we will call TRUST1. There are different versions of trust1, all of which lead to different levels of the behavior associated with this neuropeptide on male behavior. Give some examples where it would be a good idea to know a particular males genotype-that is, which of the trust1 genes he has. Give an example of when you think science has gone too far and this information should not be known.a) What is the KDD for this myoglobin variant? b) What is the predicted fractional saturation for the last box in the table? (please show your work so I can better understand) c) What is unexpected about the binding curve above? (5 words or less) d) What must be structurally different about this new variant relative to other known Myoglobin variants to generate this graph?18 Actin can be used as a loading control in a western blotting experiment. What is the purpose of a loading control?
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- PDB code 7BSJ Questions Q1 - What is the name of the protein Q2 - What does the protein do? Q3 - What are the structural features of the protein? Q4 - What are two features of your protein’s structure that make it different OR similar to haemoglobin? Q5 - Based on the structural properties of your protein, how resistant (or sensitive) would your protein be to heat denaturation and why?Effects of BPA on phosphorylation of MAPKfamily in RAW264.7 cells conclusionQuestion:- Part A) How does the molecular mechanism of elongation arrest by SRP differ between Bacillus and Mammalian systems? Please list all the differences and why. Thank you and please explain. Part B) List four interactions of the Ffh M domain in SRP mechanism.
- Drug 2-Lumacaftor (VX-809): In people with the most common CF mutation, F508del, a series of problems prevents the CFTR protein from folding into the correct shape and reaching its proper place on the cell surface. The cell recognizes the protein as abnormal and targets it for degradation before it makes it to the cell surface. In order to treat this problem, two drugs are required - an agent to get the protein to the surface and then Ivacaftor to open the channel and increase chloride transport. The drug Lumacaftor has been identified as a treatment to help with the trafficking of the protein to the cell surface. When Lumacaftor is added to Ivacaftor, the protein gets to the surface and also increases chloride transport by increasing channel opening time. For which class(es) of mutations would Lumacaftor be most effective?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.)The distal Histidine (His 64) in myoglobin is subjected to three different mutations, this is one of them: H64N. (Histidine to Aparagine) For the mutation, draw a theoretical binding curve and CO relative to the O2 and CO binding curves for wild-type Mb (see example below). Provide a clear rationale for the binding curve.