Based on the structure of CBB G-250, explain why it can bind to proteins having basic and hydrophobic amino acid residues.
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Based on the structure of CBB G-250, explain why it can bind to proteins having basic and hydrophobic amino acid residues.
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- In some proteins, the side chain of serine appears to undergo ionization. Explain why ionization would be facilitated by the presence of an aspartate residue nearby.you have the following peptide Arg-Ile-Pro-Leu-Asp-Lys-Glu The net charge on this peptide at pH 7.0 is ?. The net charge on this peptide at 1M HCl is ?.Consider the following peptide: Lys-His-Asp-Glu-Phe-Cys-Ala-Asp-His-Arg What is the net charge of this peptide at pH = 1? What is the net charge of this peptide at pH = 14?
- What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?if the tetrapeptide shown in the binding site above (Gly-Ser-His-lle) were in an aqueous solution at pH=6.2, what fraction of peptide molecules would have a +1 charge?Given the peptide Lys-Glu-Trp a) Draw the appropriate titration curve for this peptide. Label X and Y axis b) On the graph use X to mark point at which peptide have 0 net charge and Y to mark point where peptide have positive 1 net charge
- The neighboring amino acid that TYR 368 interacts with is ILE 160. What are the properties of the amino acid ILE 160?Can you please describe the specific components that each of these structures are comprised of ( alpha helices and beta sheets) in more detail? Also, what do the different colors represent? Your reply will be greatly appreciated. The ligand that was assigned to me is tadalafil.Under certain conditions, peptide bond formation is more thermodynamically favorable than peptide bond hydrolysis. Would you expect chymotrypsin to catalyze peptide bond formation?
- Given the R-groups in the peptide GLY-ASN-THR-LYS-HIS. It would most likely be: a)neither soluble nor insoluble because of the need to know the IpH of the peptide b)very water soluble because of it will easily dissolve in water c)easily associating with the water environment because it can H-bond and form dipole-dipole interactions with water d)insoluble in water because the rest of the carbon content of the peptide will not interact with waterShown to the right is a cartoon image of ETC Complex I from Y. lipolytica. A group of authors studied this wild type Complex I and also a version where the arginine at position 121 in the chain 3 subunit was mutated to a methionine (R121M). Part of chain 3 subunit contains the peptide sequence SMITH a. Draw the titration curve for the SMITH peptide. Mark all pKa’s and the pI on your curve. For the SMITH peptide at physiological pH, explain what types of interactions you believe the side chains are or are not able to participate in.Arginine exists in two high-pH forms instead of the usual one. Explain why.