Consider the tripeptide phenylalanylcysteyl methionine. Part: 0 / 2 Part 1 of 2 Draw the structure of this tripeptide at physiological pH. Click and drag to start drawing a structure. : ☐
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- MATHEMATICAL Calculate the isoelectric point of each of the following amino acids: glutamic acid, serine, histidine, lysine, tyro- sine, and arginine.Using the Nernst equation, calculate the equilibrium potential for Ca2 and for C1 from the following sets of data: a. Given [ Ca2+ ]0=1mM,[ Ca2+ ]i=100nM, find Eca2+ b. Given [ Cl- ]0=110mM,[ Cl- ]i=100mM, find Eclb. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Denote the point in the pathway in which each individual is blocked.
- a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein E. To determine where the block in protein-E production occurred in each individual, the various intermediates were given to each individuals cel Is in culture. After a few weeks of growth with the intermediate, the cells were assayed for the production of protein E. The results for each individuals cells are given in the following table. A plus sign means that protein E was produced after the cells were given the intermediate listed at the top of the column. A minus sign means that the cells still could not produce protein E even after being exposed to the intermediate at the top of the column. Draw the pathway leading to the production of protein E.Polypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant chaperone protein might be responsible for a genetic disorder involving an enzyme.Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
- REFLECT AND APPLY An inhibitor that specifically labels chymotrypsin at histidine 57 is N-tosylamido-L-phenylethyl chloromethyl ketone. How would you modify the structure of this inhibitor to label the active site of trypsin?MATHEMATICAL Sketch a titration curve for the amino acid cysteine, and indicate the pKa values for all titratable groups. Also indicate the pH at which this amino acid has no net charge.Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
- The Energetic Cost of Peptide Elongation How many ATP equivalents are consumed for each amino acid added to an elongating polypeptide chain during the process of protein synthesis?MATHEMATICAL Sketch a titration curve for aspartic acid, and indicate the pKa values of all titratable groups. Also indicate the pH range in which the conjugate acid-base pair +1 Asp and 0 Asp will act as a buffer.