EPAP in ASV is used to control

Question 1 (5 points) The titration curve for Histidine is shown here.    Question 1 refers to this titration curve.  Answer the following questions with the letter on the curve that signifies the correct position on the curve.  (1 pt. each)  Image Description  The graph titled “Histidine Titration” illustrates the titration curve of histidine, depicting the relationship between pH and the equivalents of OH⁻ (hydroxide ions) added. The x-axis represents the equivalents of OH⁻ added, ranging from 0 to 3.0, and the y-axis represents the pH, ranging from 0 to 12. Key points labeled A, B, C, D, E, and F mark significant stages in the titration process. Point A, at approximately pH 2, corresponds to the fully protonated form of histidine. Point B, around 0.5 equivalents OH⁻ and pH 3, represents the first buffering region where the carboxyl group (COOH) is being deprotonated to COO⁻. Point C, at around 1.0 equivalents OH⁻ and pH 6, indicates the first equivalence point where the carboxyl group is fully deprotonated. Point D, around 1.5 equivalents OH⁻ and pH 8, marks the second buffering region where the imidazole side chain begins deprotonation. Point E, at around 2.0 equivalents OH⁻ and pH 9, represents the second equivalence point where the imidazole side chain is fully deprotonated. Finally, Point F, at around 3.0 equivalents OH⁻ and pH 11, indicates the stage where the amino group is deprotonated. 

This figure shows the fraction or percent of myoglobin or hemoglobin O2 binding sites occupied on the Y-axis as a function of O2 partial pressure shot on the x-axis. The middle Hb blue curve is for normal Hb. The right-hand red Hb curve reflects the shift in the bonding affinity of Hb in response to a drop in pH, whereas the left-hand green Hb curve reflects the change in response to an increase in pH.     Diagram citation Wikimedia Commons (Public Domain)  Image Description  Graph depicting hemoglobin oxygen saturation percentage against oxygen partial pressure (mmHg). Three curves represent different pH levels: green for pH 7.8 (alkalosis hypocapnia), blue for pH 7.4 (normal), and red for pH 7.0 (acidosis hypercapnia). The y-axis ranges from 0 to 100%, indicating hemoglobin oxygen saturation, while the x-axis ranges from 0 to 120 mmHg, indicating oxygen partial pressure. The curves show the relationship between oxygen binding and blood pH. Which of these curves shows the greatest affinity for O2? (1 pt.) Which one of the two shifted Hb curves, right or left, would result in the release of the most O2 to the cells, if the lung pO2 decreases from 100 torr to 60 torr and the pO2 of the tissues remains the same at 27 torr? Briefly justify your answer. (2 pts.)

V-8 peptidase is an endopeptidase isolated from a strain of Staph. Aureus that cleaves a peptide bond on the carboxy side of acidic residuesin 50mM ammonium carbonate buffer at pH 8 . Treatment of peptides similar to the rattlesnake peptide with V-8 peptidase proceeds slowly, taking about 24 h to completely cleave or cut the peptide. However, if dithiothreitol (DTT) is added to the reaction in a 20 fold molar excess or BME (

An auditor selected items for test counts from the client’s warehouse during the physical inventory observation. The auditor then traced these test counts into the detailed inventory listing that ultimately agreed to the financial statements. This procedure most likely provided evidence concerning management’s assertion of

In the following procedure, the protein of interest, CA, is initially concentrated by precipitation from a 30% saturated ammonium sulfate solution. If you were interested in using ammonium sulfate precipitation to isolate a highly charged peptide, would you expect the peptide to precipitate from a low or high concentration ammonium sulfate in solution?  Briefly justify your answer.   Procedure from the reference cited below: “Briefly, cells expressing the wild-type CA protein were lysedthrough a microfluidizer. Soluble CA protein in the clarifiedlysate was concentrated by precipitation from 30% saturatedammonium sulfate. CA protein was redissolved in 50 mM Tris(pH 8.0) and functionally purified by the addition of sodiumchloride to a final concentration of 2.5 M. After two rounds offunctional purification, the wild-type CA protein wasresuspended in 50 mM sodium phosphate buffer (pH 7.5)and dialyzed against the same buffer. The dialyzed sample wasfurther purified by a subtractive anion exchange chromatography step using a Q-HP HiTrap column (catalog no. 17-1154-01, GE Healthcare, Piscataway, NJ). Purification of 2Mut and 4Mut CA mutants followed thesame protocol that was used for wild-type CA except that200 mM β-mercaptoethanol was included in all buffersthroughout the process. The functionally purified capsidmutant proteins were redissolved in 50 mM Tris (pH 7.5) and40 mM β-mercaptoethanol prior to dialysis in the same buffer,and a subsequent purification with subtractive anion exchangechromatography was performed.” A Trimer of Dimers Is the Basic Building Block for Human Immunodeficiency Virus-1 Capsid Assembly.

Which of the following is typically the auditors’ initial procedure performed to identify litigation, claims, and assessments?

A paragraph in the Opinion Section of the auditors’ report states: “In our opinion, with the exception of the effects of not observing inventory in one of the client’s Siberian warehouses, … the financial statements present fairly, in all material respects…” This paragraph expresses a(n)

Glycine is acetic acid (ethanoic acid) with an amine group attached i.e. 2-amino acetic acid. The pKa of the glycine carboxyl group is 2.34 and the pKa of acetic acid is 4.75.  Briefly explain why there is such a large difference in the pKa values between these two carboxylic acid groups.

How many residues contain sulfur? Identify these amino acids.