At what pH would the peptide, EDCY, bind to a cation-exchange resin. Recall that a cation-exchange resin function to exchange cations and are negatively charged. A. pH= 1.8 B. pH= 4.3 C. pH= 6.4 D. ph= 8.7 E. pH= 10.6.
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Proteins
We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains thousands and thousands of proteins, each with specific functions. Some help in the formation of cellular membrane or walls, some help the cell to move, others act as messages or signals and flow seamlessly from one cell to another, carrying information.
Protein Expression
The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry, and protein research laboratories.
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- For the amino acid tryptophan: Draw its complete protonic equilibria. Indicate the net charge of each form and encircle the zwitterionic form. Provide labels (A, B, C, etc.) for each form. b. Calculate the IpH of the amino acid. c. At what pH range(s) it can act as a buffer? d. What will be the predominant form(s) of the amino acid at pH (i) 1.5; (ii) 3.0; (iii) 4.5; (iv) 6.0; (v) 7.5 and (vi) 9.0?For the following peptide: group 3 C-NH, CH, H 4 group 1 HO. NH, group 4 N N-H group 2 At which pH will this structure remain stationary in an electric field? O A. when the pH is midway the pKas of groups 1 and 2 O B. when the pH is midway the pKas of groups 3 and 4 OC. when the pH is midway the pKas of groups 2 and 4 D. when the pH equals the pKa of group 1 OE. when the pH equals the pKa of group 4For the amino acid arginine: Draw its complete protonic equilibria. Indicate the net charge of each form and encircle the zwitterionic form. Provide labels (A, B, C, etc.) for each form. b. Calculate the IpH of the amino acid. c. At what pH range(s) it can act as a buffer? d. What will be the predominant form(s) of the amino acid at pH (i) 1.5; (ii) 3.0; (iii) 4.5; (iv) 6.0; (v) 7.5 and (vi) 9.0?
- A biochemist wants to separate two peptides by ion-exchange chromatography. At the pH of the mobile phase to be used on the column,one peptide (A) has a net charge of −3 due to the presence of more Glu andAsp residues than Arg, Lys, and His residues. Peptide B has a net charge of+1. Which peptide would elute first from a cation-exchange resin? Whichwould elute first from an anion-exchange resin?(E) Consider an amino acid that has one -amino group (pKa = 9.2), one -carboxyl group (pKa = 1.7) and one ionizable side chain (pKa = 6.2). At which pH range/s would this amino acid be effective as a buffer? If the amino acid shows a net charge of -1 at pH 11 and a net charge of +1 at pH 4, what pKa values would you use to calculate the isoelectric point? At what pH would the net charge be equal to zero?a. Draw the peptide chain (indicate if it is solid or hatched wedges) for the following: Glycine-(L)-Arginine-(D)-Proline-(L)-Glutamic Acid b. Compute for the isoelectric point. Show solution.
- Draw the structural form of valine that predominates in solution at each of the following ph values: a. ph<pi ; b. pl ; c. ph>pi pk values: pk 1=2.2 ; pk2 = 9.7 Do also for asp (1.88, 9.60, 3.65) and lys (2.88, 8.95, 10.53)Two peptide sequences are shown below.Peptide A: N-term – GDL – C-termPeptide B: N-term – GTL – C-terma. Draw each peptide at physiological pH. Circle each ionizable functional group in your drawing.b. Briefly explain why changing aspartate to threonine changes the number of ionizable functionalgroups in the peptide chain.c. Briefly explain why the functional group found in aspartate’s side chain is ionizable but the functionalgroup found in threonine’s side chain is not.Given the amino acids below, what amino acid will elute first in a cation-exchange column. 1. Aspartate or Lysine using a buffer at pH 7 2. Arginine or Methionine using a buffer at pH 7 3. Lysine or Valine using a buffer at pH 7 4. Glycine or Valine using a buffer at pH 7 5. Serine or Alanine using a buffer at pH 7
- The following peptides were separated using ion-exchange chromatography based on the use of an anion exchange resin. Which peptide was eluted first? A B Peptide Name A B C D Molecular Weight (g/mol) 360 1080 1800 1440 Peptide Net Charge -2 -1 0 +1Mixtures of amino acids can be analyzed by first separating the mixture into its components through ionexchange chromatography. Amino acids placed on a cation-exchange resin containing sulfonate ( -SO3-) groups flow down the column at different rates because of two factors that influence their movement: (1) ionic attraction between the sulfonate residues on the column and positively charged functional groups on the amino acids, and (2) aggregation of nonpolar amino acid side chains with the hydrophobic backbone of the polystyrene resin. For each pair of amino acids listed, determine which will be eluted first from the cation-exchange column by a pH 7.0 buffer. (a) Aspartate and lysine (b) Arginine and methionine(c) Glutamate and valine (d) Glycine and leucine (e) Serine and alanineWhich of the following statements are TRUE? Multiple answers:Multiple answers are accepted for this question PLEASE SHOW WORK FOR EACH PART AND EXPLAIN WHY EACH ANSWER CHOICE IS WRONG OR RIGHT a. The tripeptide His-Lys-Glu has a net charge of -2 at pH 8.0. b. The tripeptide Asp-Asp-Asp has a net charge of -3 at pH 7.0. c. The tetrapeptide His-His-His-His has a net charge of -1 at pH 7.0. d. There are 6 possible sequences for a tripeptide containing Arg - His - and Pro. e. Certain bacteria synthesize cyclic tetrapeptides. The net charge at pH 7.0 of a cyclic tetrapeptide consisting of two Pro and two Tyr is 0.