Draw a titration curve for the tetrapeptide Trp-Asp-Lys-Gly. Label all pK,s, the pl and the net molecular charges at pH 1 and pH 14 on the graph with their values.
Q: A typical amino acid with one amino group and one carboxylicacid group, such as serine, can exist in…
A: At lower pH that means in acidic conditions the carboxylate ion takes up proton and exists as…
Q: A typical amino acid with one amino group and one carboxylic acid group, such as serine can exist in…
A: At lower pH that means in acidic conditions the carboxylate ion takes up proton and exists as…
Q: Calculate the volume of saturated Ammonium sulphate to be added to a 276ml of protein solution to…
A:
Q: The pKa values of the conjugate acids of 2-aminopyridine (6.71) and 4- aminopyridine (9.11) are as…
A: It is given that 2-amino pyridine conjugate acid has a pKa value of 6.71 and 4-aminopyridine…
Q: what is the purpose of hydroxylamine hydrochloride in the spectrophotometric determination of iron…
A: Iron is determined sphetrophotometrically in FAS, ferric ammonium sulphate [NH4Fe(SO4)2.12H2O]. Iron…
Q: Below is the structure of a hypothetical photo-affinity probe analogue of the anti- malarial drug…
A: Cross-links with nearby proteins in the presence of UV light. B is the correct answer.
Q: Fig. 1 shows the possible effect of pH on recovery and impurity removal at the selection of a…
A: The Y-axis of the graph represents the percent recovery of the impurity, and the X-axis of the graph…
Q: 2. 1 M valine is present in 1 liter of water at (a) pH 7.5, (b) pH 2.5. For each functional group,…
A: Valine is a nonpolar amino acid with the uncharged structure shown below:
Q: Using this info, please calculate two theoretical yields for (1) p-acetamidobenzenesulfonamide and…
A:
Q: The first step in the procedure asks you to prepare five dilutions of the protein standard (BSA) in…
A: During the dilution process, solvent is added to the solution and hence changing the concentration…
Q: What is the possible identity of the amino acid? [Select] What is the isoelectric point of AA?…
A: Since you have posted a question with multiple sub-parts, we will solve first three subparts for…
Q: What is the effect of discolored AgNO3 on the concentration of KSCN?
A: We have to tell the effect of discolored AgNO3 on the concentration of KSCN.
Q: A sample containing histidine (pKas 1.8, 6.0, 9.3), lysine (pKas 2.2, 9.1, 10.5), and leucine (pKas…
A: Because a protein's net charge is pH-dependent, the sample may be eluted from IEX medium by varying…
Q: A purified protein is in a HEPES (N-(2-hydroxyethyl)piperazine-N-(2-ethanesulfonic acid)) buffer at…
A: Given: concentration of NaCl = 600 mM Since, 1 mL of sample, 600 mM NaCl and HEPES buffer is…
Q: Consider an amino acid with the following pKa values: pKa1 = 2.71 and pK, = 9.31 At what pH value in…
A: Amino acids are amphoteric in nature due to the presence their ionizable α-amino and α-carboxylic…
Q: At pH 5.0? Q2) (a) Draw the structure of the predominant form (principal species) of…
A:
Q: A chromatogram showing the results for an amino acid test show a solvent line of 7.5cm. If the amino…
A:
Q: For acetate with a pKa of roughly 4.2, what is a lowest pH where this molecule could serve as a good…
A: Given the pKa value of the buffer, pKa = 4.2 According to Henderson equation: pH = pKa + log[A-][HA]
Q: The electrophoresis of a sample containing 2-amino-4-methylpentanoic acid. (pKa of a-COOH = 2.2, pKa…
A:
Q: What is the K, of the amino acid leucine if it is 34.5% disso- ciated at pH = 9.46? |3D
A: “Since you have asked multiple question, we will solve the first question for you. If you want any…
Q: Calculate the pH at each of the following points for the titration of 200 mL of 0. 45 M dl-Histidine…
A: Initially, we have 200 mL of 0.45 M dl-Histidine. Initial mmoles of dl-Histidine = C*V= 0.45…
Q: they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively.…
A: For comparison association constant of each is determined. The one having highest value of…
Q: Why is Bromocresol green used for the base unknown while phenolphthalein is used for the acid…
A: Phenolphthalein is a colourless, weak acid which dissociates in water forming pink anions. The Pka…
Q: A protein with a pI of 7.5 will be purified using ion-exchange chromatography. Which ion exchange…
A: b) A resin with sulfonic acid group is the correct option.
Q: To establish 50% ammonium sulfate saturated solution, 314 g/l of salts should be added. Calculate…
A: It is given in question that solubility of salt is 314 g/L. This means 314 g of salt is soluble in…
Q: Calculate the pH at each of the following points for the titration of 100 mL of 0. 6 M dl-Histidine…
A: A triprotic acid is one that can dissociate to furnish three protons by three equilibrium equations.…
Q: What are the structures of threonine in each part of its titration curve? Give a clear handwritten…
A:
Q: What are the chief differences between the Ninhydrin and Bradford assays for amino acid…
A: Ninhydrin and Bradford assay both are performed to determine amino acids. Nin hydrin reacts with…
Q: What is the fraction of EDTA at pH 10.7?
A: The concentration of hydrogen ion in the solution at the 10.7 pH is determined as follows.
Q: Based on the graph, the retention of 4-aminobenzoic acid is not affected changes in mobile phase pH…
A: 4-amino benzoic acid remains in zwitterionic form in ph range 2-9 (approx) so on changing ph of…
Q: For the determination of Pb in blood, a 5.00 mL sample was treated with trichloroacetic acid to…
A: The given data is as follows. A1 = 0.396 (first point) A2 = 0.599 (second point) C1 =…
Q: While purifying a new protein using a dextran Sephadex, the consistency of the column material…
A: As per the bartleby expert guidelines, I am allowed to answer one question at a time . Please…
Q: For two samples of cocaine, A was made up in an aqueous solution of pH 2.8, while B was made up in…
A: Given:- The cocaine is the base due to tertiary amine group as a base. Therefore in…
Q: N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic A purified protein is in a Hepes acid) buffer at…
A:
Q: The pka of ascorbic acid is 4.2 at 24C. At what pH is the ratio of the deprotonated form to the…
A: Henderson Hasselbach equation is pH=pKa+log[deprotonated form][protonated form]
Q: If prior to the analysis, the protein X needs to be solubilised in 250 mM acetate buffer, pH 4.0 to…
A:
Q: Question attached
A: Paper chromatography is a qualitative method in order to detect the presence of colored components.…
Q: Cysteine is an amino acid with S as the donor atom. It forms complexes with Fe2*, Hg2*, Mg²*, and…
A: The donor atom at cysteine residue is S.
Q: what is The method that would be BEST to use to monitor protein secondary structure during the…
A: The secondary structure of the protein is affected by the complex folding properties of the protein…
Q: and K2 = 5.42 x 10. In a solution made by dissolving 25.00 g of oxalic acid in enough water to a…
A:
Q: Enz-SH + Ag* –→ Enz-S-Ag + H* The affinity of Ag* for sulfhydryl groups is so great that Ag* can be…
A: The detail explanation is given below
Q: 65mL of a 0.2M solution of the tetrapeptide Arg-His-Ile-Glu is adjusted to pH=7.8. The solution is…
A: Here, we are titrating a tetrapeptide Arg-His-Ile-Glu against HCl.
Q: How does the shape of a titration curve confirm the fact that the pH region of greatest buffering…
A: As there are three question are present I answered only one. you can repost your remaining two…
Q: 1) Compare between three steps for Kjeldahl method for determination of protein?I
A: INTRODUCTION: Kjeldahl method is defined as the method which is used for quantitative determination…
Q: A purified protein is in a HEPES (N-(2-hydroxyethyl)piperazine-N-(2-ethanesulfonic acid)) buffer at…
A: Initial concentration of NaCl solution, Minitial = 600 mM Initial volume taken, Vinitial = 1 mL…
Q: The pKa values for the α-carboxylic acid and the α-amino acid groups is cysteine are 1.092 and…
A:
Q: The peptide below is placed into a buffer with a pH = 1.54 -NH-CH-C HO- H;N-CH- CH2 -NH -CH-C…
A: We have to find out the direction of movement of peptide at pH=1.54
Trending now
This is a popular solution!
Step by step
Solved in 8 steps with 7 images
- Sketch a titration curve for the amino acid cysteine, and indicate the pKavalues for all titratable groups. Also, indicate the pH at which cysteinehas no net charge.4. Proteases are enzymes that catalyze the hydrolysis of peptide bonds in proteins. The enzyme trypsin is a protease that specifically hydrolyzes only those peptide bonds that are formed by the carboxyl group of basic amino acid residues. Trypsin is present in the small intestine where it functions at an optimum pH of 8. Consider the pentapeptide Phe-His-Val-Lys-Glu. Draw the structures of the products formed from trypsin-catalyzed hydrolysis of this peptide.An alpha carboxylic acid group (COOH) of protein amino acids has a pka = 2.4. The ratio of %3D dissociated versus undissociated molecule (CO0-/COOH) at pH = %3D 2.4 will be
- Draw all of the structures of cysteine as the pH increases from low to high, then sketch a titration curve that best represents the titration of cysteine. in the curve, label each: x-axis, y-axis, pKa (COOH), pKa (NH3+), pKa(R-group), and the calculated pI value.Write general equations showing the ionization of a protein in acid medium and in basic medium. What medium favors acid ionization? Basic ionization?Give typed full explanation not a single word hand written otherwise leave it Calculate the isoelectric point of the amino acid histidine by plotting the titration curve. (pka values α-COOH=1.82, α-NH2= 9.17, imidazole= 6.0)
- Attempt titrating an amino acid against a weak base and discover the numberof dissociating ( ionizable ) functional groups in the amino acid.A purified protein is in a HEPES (N-(2-hydroxyethyl)piperazine-N-(2-ethanesulfonic acid)) buffer at pH 7 with 600 mM NaCl. A 1 mL sample of the protein solution is placed in a tube made of dialysis membrane and dialyzed against 2.0 L of the same HEPES buffer with 0 mM NaCl. Small molecules and ions, such as Na, Cl, and HEPES, can diffuse across the dialysis membrane, but the protein cannot. Once the dialysis has come to equilibrium, what is the concentration of NaCl in the protein sample? Assume no volume changes occur in the sample during the dialysis. [NaCI] = mM If the original 1 mL sample were dialyzed twice, successively, against 200 mL of the same HEPES buffer with 0 mM NaCl, what would be the final NaCl concentration in the sample? [NACI] = mMDraw the structure of glycine that will predominate at the pH=1.5pH=1.5 (pI=6.0)(pI=6.0). Look at screenshot
- A solution of two diastereomers contains 88.6% of (3S,4S)-tert-butyl-3-amino-4- hydroxypyrrolidine-1-carboxylate and 11.4% of (3S,4R)-tert-butyl-3-amino-4- hydroxypyrrolidine-1-carboxylate. Calculate the percent diastereomeric excess (%d.e.) of the (3S,4S)-tert-butyl-3-amino-4- hydroxypyrrolidine-1-carboxylate in this solution.Draw a titration curve for the following peptide and circle the region(s) where this peptide would be a good buffer. Label the location on the titration curve where the peptide is least soluble: H-A-I-YSketch the titration curve of CRIP and draw the corresponding predominant structue at each equivalence point. Determine: 1) PI 2) Charge of the peptide above at pH 10 3) Charge of the peptide above at pH 24) Charge of the peptide above at around 12.5?