Within the picture below, click or tap on the letter (A, B, C) that labels the binding curve for myoglobin.
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Letter "A" represents binding curve for myoglobin.
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- resting state of the protein, the Lys 216 Schiff base has pKa = 9.5 and Asp 85 has pKa = 3.5. When the conformational change occurs, the proton that was on the Schiff base moves to Asp 85. This should tell you that one or both of these two pKas changed with the conformational change. How does the pKa of Asp 85 compare with the pKa of the Lys 216 Schiff base after the conformational change?Choice and Preparation of a Buffer System1. Choosing the proper buffer solution In Protein Precipitation, two liters of 5mM buffer solution with pH 5.2 is needed in the isolation of albumin. Which among the following buffer solution is best fitted for said purpose? Justify your answer.Buffer solutions pKa Acetate buffer 4.73Tris- (hydroxymethy) aminomethane 8.08Phosphate buffer 7.20 2. Preparation of the chosen buffer system Calculate and measure the amounts (in grams if solid and in mL if liquid) of weak acid and conjugate base needed to be able to prepare the chosen buffer system in part A above. Express your answer in useful units (that is, prepare it from practical amounts or concentrations of starting materials).Activity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1 Alanyl-phenylalanine 2. Lysyl-alanine 3.Phenylalanyl-tyrosyl-leucine
- Need help, please. Draw an oxygen binding curve of Hb at a pH of 7.4 and another curve where all 2,3 BPG has been removed Draw an oxygen binding curve of Hb at a pH of 7.4 and another at pH. Draw an oxygen binding curve of Hb at a pH of 7.4 and another with a mutant Hb in which the predominant form of the protein is monomericActivity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1. Glycyl-valyl-serine 2. Threonyl-cysteine 3. Isoleucyl-methionyl-aspartateCrystal structures exist for three neurokinin-1 (NK1) ligand complexes with the following pdb codes (6hll, 6hlo, 6hlp) For each of the three crystal structures identify four amino acids in the NK1 binding site that contact the ligand indicating both the residue type in three letter code and the residue number. One of the chose amino acids should form a hydrogen binding interaction to the ligand, state which functional group the amino acid utilises in each case
- Crystal structures of neurokinin-1 with pdb codes 6hll, 6hlo, 6hlp. Which is the highest quality crystal structure?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.MATHEMATICAL The hydrolysis of a phenylalanine-containing peptide is catalyzed by -chymotrypsin with the following results. Calculate KM and Vmax for the reaction. PeptideConcentration(M)Velocity(Mmin1)2.51045.010410.010415.01042.21065.81065.91067.1106
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