5 (a) Describe in detail how you will determine the primary structure of protein. (c) You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows: Histidine 7.64 Lysine 9.74 Cystenie 5.02 Show how you will separate the mixxture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.

5 (a) Describe in detail how you will determine the primary structure of protein. (c) You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows: Histidine 7.64 Lysine 9.74 Cystenie 5.02 Show how you will separate the mixxture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.

Chemistry: Principles and Reactions

8th Edition

ISBN:9781305079373

Author:William L. Masterton, Cecile N. Hurley

Publisher:William L. Masterton, Cecile N. Hurley

Chapter23: Organic Polymers, Natural And Synthetic

Section: Chapter Questions

Problem 44QAP: A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of...

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A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)
(a) Describe in detail how you will determine the primary structure of protein. (b)You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows:Histidine 7.64Lysine 9.74Cystenie 5.02Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows:Histidine 7.64Lysine 9.74Cystenie 5.02Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture
(a) Describe in detail how you will determine the primary structure of protein. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows: Histidine 7.64 Lysine 9.74 Cystenie 5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows:Histidine 7.64Lysine 9.74Cystenie 5.02i. Show how you will separate the mixture into the pure forms. ii. State and describe any instrument that you will use to separate the components in the mixture
The isoelectric point (pl) of phenylalanine is pH 5.5. Draw the structure of the major form of glutamic acid at pH values of (a) 1 (b) 5.5 (c) 11.0.
The activity of an enzyme requires a glutamic acid to display its -COOH functional group in the protonated state. Suppose the pK, of the -COOH group is 4.07. (a) Will the enzyme be more active at pH 3.5 or 4.5? Explain. (b) What fraction of the enzymes will be active at pH = 4.07? Explain. (c) At what pH will the enzyme show 78% of maximal activity?
Answer the following questions on the basis of the free energies of formation at 25°C shown in the table at the top of the next page: (a) Does the peptide bond between alanine and glycine form spontaneously under standard conditions?
Two different proteins X and Y are dissolved in aqueous solutionat 37 °C. The proteins bind in a 1:1 ratio to form XY. Asolution that is initially 1.00 mM in each protein is allowedto reach equilibrium. At equilibrium, 0.20 mM of free X and0.20 mM of free Y remain. What is Kc for the reaction?
A typical amino acid with one amino group and one carboxylicacid group, such as serine, can exist in water in several ionic forms. (a) Suggest the forms of the amino acidat low pH and at high pH. (b) Amino acids generally havetwo pKa values, one in the range of 2 to 3 and the other inthe range of 9 to 10. Serine, for example, has pKa values of2.19 and 9.21. Using species such as acetic acid and ammoniaas models, suggest the origin of the two pKa values.(c) Glutamic acid is an amino acid that has threepKa's: 2.10, 4.07, and 9.47. Draw the structure of glutamicacid, and assign each pKa to the appropriate part of themolecule. (d) An unknown amino acid is titrated withstrong base, producing the following titration curve.Which amino acids are likely candidates for the unknown?
Given the Ka values (in parentheses) for the following acids: HSO4– (Ka= 1.2 x 10–2); HNO2 (Ka= 4.0 x 10–4); HC2H3O2 (Ka= 1.8 x 10–5); Calculate Kc values for the following acid-base equilibria: (a) HSO4–(aq) + C2H3O2–(aq) ⇌ HC2H3O2(aq) + SO42–(aq) (b) HC2H3O2(aq) + NO2–(aq) ⇌ HNO2(aq)+ C2H3O2–(aq)
All amino acids have two ionizable functional groups: an a-amino group (average pK, of 9.4) and an a-carboxylic acid group (average pK, of 2.2). Glutamic acid has an ionizable side chain (R group) with a pK, of about 4.1. One of the possible ionization states of glutamic acid is shown in the image. H₂N-CH-C-OH CH₂ At what pH would this structure of glutamic acid be the predominant ionization state? Consider the ionization state of all three of the functional groups. OH The protonated form of the R group of glutamic acid is shown in the structure. The ratio of the protonated form to the charged (deprotonated) form depends on the pK, of the R group and the pH of the solution. 2.6 4.1 1.5 Select the pH values at which the charged form of the R group would predominate. 7.0 11.3