If prior to the analysis, the protein X needs to be solubilised in 250 mM acetate buffer, pH 4.0 to maintain its structural integrity. How would you take this
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) Illustrate a titration curve of the following structure. (Solid lines indicate covalent bonds)…
A: Since you have posted a question with multiple sub-parts, we will solve first three subparts for…
Q: How does the polarity of the amino acid affect its elution within the paper stationary phase?
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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: 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: d. When 99% of glycine is in its -NH3* form, what is the pH of solution due to it's amino group?…
A: 99% of glycine is in its -NH3+ form, so we have
Q: Calculate the volume of saturated Ammonium sulphate to be added to a 112ml of protein solution to…
A: Here, we are performing dilution of given protein solution. So, C1V1 = C2V2 Where ,C1 and V1 are…
Q: viii) You have the following stock solutions available: 2.5M Tris, 0.5M Glycine and 10% SDS, how…
A: To prepare 1 liter solution of 25mM tris, 190mM glycine and 0.1% SDS can be prepared by following.
Q: Consider an amino acid (A) with no ionizable side chains, and call the three species involved in the…
A: Using Hendesen-Hasselbalck equation pH = pKa + log([HA]/[H2A+]) with, [HA] + [H2A+] = 1 mM [HA] = 1…
Q: The initial pH of a 2M arginine solution is 14. What is the predominant structure of arginine in…
A: At pH = 14 , arginine exists in completely deprotonated form .
Q: For lysine and arginine, the isoelectric point, pI, occurs at a pH where the net charge on the…
A: The isoelectric point for the amino acid Lysine can be calculated by using the pKa values of α-amino…
Q: Calculate the volume of saturated Ammonium sulphate to be added to a 201ml of protein solution to…
A: Interpretation - Calculate the volume of saturated ammonia sulfate to be added to a 201mL of…
Q: The amino acid His is triprotic with pK1 (α-COOH) = 1.82, pK2 (α-NH3+) = 9.17, and pK3 (side chain)…
A: If the pKa of acid is equal or lower than the pH of the solution then the acid will get deprotonated…
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: 4b) Canavanine is closely related to arginine, and like arginine its side group has a +1 charge when…
A: Canavanine has a similar structure of Arginine. Hence Canavanine has 3 groups that can be…
Q: Explain why the pI of lysine is the average of the pKa values of its two protonated amino groups.
A: First the lysine structure is noted as follows,
Q: Sketch a titration curve for the following amino acids and indicate the pKa values for all…
A: Answer -
Q: Rank the amino acids used in the experiment in Part II in the order of increasing solubility in…
A: The solubility of amino acids, generally, depending upon the nature of the side chain and they are…
Q: The pKa values of the carboxylic acid groups of oxaloacetic acid are 2.22 and 3.98.a. Which carboxyl…
A: a. The structure of oxaloacetic acid is; The pKa value is inversely related to the acidic strength…
Q: At pH 5.0? Q2) (a) Draw the structure of the predominant form (principal species) of…
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Q: Give the numbers of peptide bond present in given structure, structure is given at pH 10.5, find…
A: The CO- NH bond is called peptide bond. A peptide bond connects two Amino acid units. Amino acid…
Q: Where is the effective buffering range for this amino acid in the acidic region?
A: Buffer is the solution that resists change in pH when small amount of acid or base is added to it.…
Q: (b) Describe how the charge of some amino groups in a protein might differ at pH 9.0 and pH 5.0.…
A: Polypeptides are polymers of amino acids that make up proteins. The amino (–NH2) and carboxylic acid…
Q: Consider a buffered solution with a pH of 11 that contains tyrosine as a free amino acid. W the net…
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Q: Tyrosine is an amino acid whose side chain has a pKa of 10.1. At pH 7, what protonation form would…
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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: Discuss the principles of the colorimetric and enzymatic methods for quantitating uric acid.
A: Generally there are two methods of quantitating uric acid . Colorimetric method Enzymetic method
Q: Write general equations showing the ionization of a protein in acid medium and in basic medium.…
A: Structure of protein : NH2 -R-COOH NH2 = Basic groupCOOH = Acidic groupR= Alkyl or Aryl group 1.…
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: The state of ionization of a specific amino acid is directly influenced by the pH of the surrounding…
A: The state of ionization depends upon the pH of the medium. Lysine is a basic amino acid having two…
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: 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: Valine has pKa's of 2.286 and 9.719. Estimate the fractional composition of Valine in the -1 form at…
A: Amino acids are amphoteric in nature due to the presence their ionizable α-amino and α-carboxylic…
Q: What is the name of this oligopeptide? Use the three letter and one letter nomenclature of the amino…
A: Two amino acids are linked to each other through a peptide bond [C(=O)-NH-]. Hence "n" number of…
Q: Draw the sequential transition of glutamic acid as it passes from its fully protonated form to its…
A: The biomolecules in which carbon atom is bonded to carboxylic group, amine group, alkyl group and…
Q: N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic A purified protein is in a Hepes acid) buffer at…
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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: Complete the table for the ionizable groups of the fictitious amino acid hypothetinine. pKa (to TWO…
A: The correct answer is given
Q: Question attached
A: Paper chromatography is a qualitative method in order to detect the presence of colored components.…
Q: When analyzing a PTH (phenylthiohydratoin) derivative of the amino acid isoleucine, resulting from…
A: Reversed-Phase Chromatography: It is a liquid chromatography technique that involves the separation…
Q: For the amino acid alanine, the major species in solution at pH 7 is the zwitterionic form, which…
A: Here, we have to estimate the ratio of the concentration of the neutral amino acid species to the…
Q: For aspartic and glutamic acids, the isoelectric point occurs at a pH where the net charge on the…
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Q: A solution of amino acid having carboxylic side chain was titrated against NaOH. If initial pH of…
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Q: The pKa values of the carboxylic acid groups of oxaloacetic acid are 2.22 and 3.98. a. Which…
A: a. The structure of oxaloacetic acid is; The pKa value is inversely related to the acidic strength…
Q: Sketch a titration curve for gly-val and indicate the pKa values. Also indicate the pH at which this…
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Q: For the amino acid glutamate, what fraction of the side-chain (R-group) will be ionized at pH = 3.5?…
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Q: Name four factors (bonds or other forces) that contribute to stabilizing the native structure of a…
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- To separate three organic compounds from an aqueous solution, one basic, one acidic and one neutral apolar, by extraction technique, create an appropriate extraction scheme by writing examples for each and write down the reactions that took place at each stage.The state of ionization of a specific amino acid is directly influenced by the pH of the surrounding medium in which the amino acid is at that time. Use the amino acid lysine and show on a rough graphical outline the transition from completely protonated to completely deprotonated.4. To perform a certain activity assay it is necessary to have 0.25 mL of an enzyme at a concentration of 0.2 mgml¹ in the presence of 0.4 mM substrate and 200 mM NaCl in a suitable buffer. The stock solutions of enzyme, substrate and NaCl are 4 mgmL-¹, 40 mM and 1 M all in the same type of buffer. What volumes of the stock solutions and buffer are required for each assay?
- Malin just discovered a new protein, Malinase and for it not to unfold and lose its function, he realized that the protein needs to be constantly immersed in a pH = 11.90 solution. He is therefore interested in preparing a 50.0 mL 0.080 M pH = 11.90 buffer to contain the protein. He listed down the acid solutions available to his disposal, and also looked for their acid dissociation constant (Ka) values. ACID 2.00 M NITROUS ACID (HNO:) 2.00 M ACETIC ACID (CH,COOH) 2.00 M ASCORBIC ACID (H:Asc) Ka: 4.00 x 10 N/A 1.76 x 105 N/A 7.90 x 10 1.60 x 102 Kaz Каз N/A N/A N/A 2.00 M PHOSPHORIC ACID (H:PO4) 7.52 x 10 6.23 x 10 4.28 x 103 A. Identify which weak acid system is best to use in preparing the buffer? Why? В. Identify the species which will make up the buffer system? C. prepare the buffer . Calculate the amount (in mmoles) of each of the components necessary to D. Indicate how Malin is supposed to prepare the buffer from 2.00 M of the acid and/or 4.00 M N2OH. E. Calculate the resulting…30ml of 0.06M solution of protonated form of anion amino acid methionine (H2A+) is treated with0.09M NaOH.calculate pH after addition of 20 ml of base.pKa1=2.28 and pKa=9.2 please answer this question .with explanationWater sample from different river water was subjected to a qualitative alkaline analysis by titrating against 0.1250 MHC1 and using phenolphthalein and bromocresol green end point. The table below shows the volumes of acid needed to titrate 25.00-mL portions of each sample and their corresponding end point, separately. Use this information to deduce the composition of the solutions. Calculate the molar concentration of each solute. Volume (mL) Phenolphthalein end Bromocresol green Solute identity concentration end point Volume (mL) Molar Sample point 22.40 of solute/s 1 22.41 2 0.00 33.40 3 15.67 42.13 4 29.64 36.42
- The concentration of ammonia in a cleaning product was determined by back titration.Firstly, 10.00 cm3 of the cleaning product was pipetted into a large conical flask,containing 250.00cm3 of 0.50 mol/l HCl to give Solution A.Following a period of reaction and shaking, 50.00cm3 of Solution A was removed anddiluted to 250 cm3 with water in a volumetric flask to give Solution B.20 cm3 samples of Solution B were titrated against 0.05 mol/l Na2CO3 solution, givingan average titre of 12.45 cm3. i) Write equations for the reactions that have taken place.ii) Determine the concentration of NH3 in the original cleaning product in mol/l,g/l, ppm, and % w/v.The sample is dissolved in a mixture containing 10ml of distilled water and 20 ml of dilute HCL.After dilution, add 50 ml of water and 1g of potassium bromide.The mixture is titrated with 0.1N NaNO2 solution . 4 drops of atropine are used as an indicator .At the last point of the titration the color change from red to yellow. Write the reaction that takes place in the nitrometer and the sulfatiazole sample indicator?Sketch a titration curve of the amino acid isoleucine with pH on the y-axis and volume of titrant on the x-axis. Label each axis appropriately. Draw the chemical structures of the 3 possible forms of isoleucine in aqueous solution. Indicate on the graph the following: where each of the species predominates, the pKa values and the isoelectric point.
- Three-point calibration was not performed on the pH meter prior to titration. Is there a positive error, negative error, no effect, or error could not be determined In terms of the Computed pKa of the unknown weak acid?A student added a total of 75 mL sodium hydroxide to titrate an amino acid solution with 0.5M NaOH. They also calculated that they added a total of 14 mL of sodium hydroxide to arrive at pH 2.6 and a total of 32 mL of sodium hydroxide to arrvive at pH 4.8.What was the initial concentration of the amino acid solution in milimolar (mM)? The calculations must be presented such that those can be recapitulated by the marker. Provide the answer with no decimal places. Show all details of your working out. State the answer in a full sentence.A student has been asked to prepare a reaction mixture, which is suitable to test the activity of an enzyme in dependence of the pH of the solution. The mixture contains a buffer compound, which will facilitate a stable pH. Now they have to determine the ratio of conjugate base/weak acid required such that they will obtain the desired pH. They have been provided with the buffer parameters provided in the image below. Determine the ratio with two decimal places precision. B_A ratio_007 Note: You may need to round the numbers to get the required answer. Previous Page Next Page Final pH of solution: 5.8 Final volume of solution: 100 ml Buffer compound concentration: 150 mM Buffer compound pk₂: 6.3 Page 4 of 12