Need questions 3 and 4 answered, please. Thank you! 3.) The enthalpy change associate with a biological process is -13200 cal/mol at 298K and +14700cal/mol at 310K. What are the values of ACp and TH?4.) A hydrogen bond can easily form between the carbonyl (C=O) of on amino acid in a protein anda H bonded to N in another part of the protein (N-H). This is often depicted (if they are colinearas:C=OH-Nbut, each of these parts of the protein can also hydrogen bond to water. When the interaction aboveforms, we say that the Hydrogen bonds with water are exchanged for a different H- bond. Sketch the Hbonds of these groups to water molecules below.C=OH-N

The heat capacity of a system is the amount of heat that must be supplied to a system to raise its…

Answered: 3.) The enthalpy change associate with…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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1)Ubiquitin is a small protein with a monoisotopic mass of 8560 Da. a) Electrospray ionization of this small protein typically results in major charge states of +8, +9, +10, +11, +12, and +13. Using this information, complete the table below, assuming the charges on each come from protonation. Report mass and m/z values to the ones place. b) Using the data you entered in the table, sketch an expected ESI-MS spectrum for ubiquitin. Label each peak with its charge state. What do you notice about the spacing of peaks along the x-axis. c)The figure shows an experimentally obtained electrospray mass spectrum for ubiquitin. Compare this spectrum to the spectrum you predicted. Are there any differences? If so, what might cause these differences?
You have an initial solution in which you added quantities of “A” and “B” such that there is 4.5 M “A” and 2.5 M “B” and no complex (“AB”) at time 0. After equilibrium, you are able to isolate and quantitate the “AB” complex, and find its concentration is 1.5 M. Given that RT is 0.59 kcal/mol, what is the delta Go’ for the association reaction?
Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.5; Pk2 = 10.8; PkR = 8.5 His: Pk1 = 1.6; Pk2 = 9.0; PkR = 7.0 Lys: Pk1 = 2.2; Pk2 = 8.5; PkR = 9.8 a.draw the protonic equilibria for the tripeptide. b.what is the IpH? c.What is the dominant structure at pH 3.0? d.What is the first buffering region of the tripeptide?
Diethylaminoethyl cellulose is a positively charged resin used in ion-exchange chromatography with a pKa is about 11. A negatively charged protein with an isoelectric point of 5.0 is applied to the column in a buffer at pH 7 and containing 0.1 M NaCl. Which of the following conditions is most likely to weaken the interaction between the protein and the resin? A Raising the pH to 8 and decreasing the NaCl to 0.05 M B Raising the pH to 8 and increasing the NaCl to 0.2 M C Lowering the pH to 6 and decreasing the NaCl to 0.05 M D Lowering the pH to 6 and increasing the NaCl to 0.2 M
You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its ΔGo for unfolding is 1.5 kcal/mol at 37o (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20-fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?
1. You want to purify a protein using anion exchange column chromatography. In this technique, the solid state beads are positively charged. What charge would you want your protein to have in order for it to "stick" to the beads? Neutral Positive Negative 2. In your anion exchange experiment, your protein of interest has a pI of 6.0. Which of the following buffer solutions would you want to use when loading your protein extract onto the column so that your protein "sticks" to the beads? pH 4.5 pH 7.3 pH 6.0 3. You want to analyze your chromatography results using gel electrophoresis. If your protein is a pentamer consisting of 2 alpha subunits, 1 beta subunit, and 2 gamma subunits, how many bands would you expect to see on your gel? The alpha subunits are 32kDa. The beta subunit is 32kDa. The gamma subunits are 15kDa. 1 5 2 3 4. You want to analyze your chromatography results using gel electrophoresis. If your protein is a pentamer…
5 You need to separate the following three proteins, Protein A (MW 76 600 Da; pI 4.5); Protein B (MW 70 000 Da and pI 8.2) and Protein C (MW 42 000; pI 8.6). Describe what column/s you would use, the pH of the buffer/s you would use, which proteins are retained on the column and how you would elute the bound protein/s. How would you monitor where the protein peaks elute and whether the protein in each peak is pure of not?
The ionization of p-nitrophenol is shown below (pKa = 7.0): a. Identify the weak acid and conjugate base. b. At pH 7, what are the relative concentrations of ionized and un-ionized p-nitrophenol? c. If enough concentrated hydrochloric acid is added to a solution of p-nitrophenol to lower the pH from 7 to 5, what will happen to the relative concentrations of the ionized and un-ionized forms? d. Ionized p-nitrophenol has a yellow color, while the un-ionized form is colorless. The yellow color can be measured using a spectrophotometer at 400nm. In order to determine the total amount of p-nitrophenol in a solution, would you perform the spectrophotometer reading at an acidic or basic pH? Clearly explain why? e. A solution of p-nitrophenol at pH 7.95 was found to have an A400 of 0.255 . What is the total concentration (in µM) of p-nitrophenol (ionized plus un-ionized) in the solution? The molar extinction coefficient of p-nitrophenol is 18,500 M-1cm-1 and the pKa is 7.
Assume that some protein molecule, in its folded native state, has onefavored conformation. But when it is denatured, it becomes a “random coil,” with many possible conformations.(a) If we only consider the change in entropy for the protein, what mustbe the sign of ΔS for the change: native → denatured? (Note: As suggestedin the next problem, this does not include solvent effects, which also make significant contributions to ΔS.)(b) How will the contribution of ΔS for native → denatured affect thefavorability of the process? What apparent requirement does this imposeon ΔH if proteins are to be stable structures?
in the Isoelectric Precipitation of Proteins: Casein from Milk - A student while performing the casein precipitation using isoelectric pH, observed maximum precipitation at a pH=3.5. What could have happened during the experiment which have led to such an observation ?
1.2. Using DEAE-cellulose as ion exchange resin, indicate the starting and ending pH for the narrowest experimental pH range used to separate an amino acid mixture consisting of Cys, His and Leu Starting pH: _____ Ending pH: _____
1. a. draw the L- & R- stereoisomer of the amino acid T using a fischer projection or a newman projection. b. draw the tripeptide LEM in the protonation state you would expect at physiological pH. show the position of phi and psi angles on the E residue

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