The structure below shows a tripeptide at physiological pH with the protonatable groups labeled with their correspondingpKa's.pKa -4.1вpka -10H3NpKa -2ApKa -3.7 öpKa -10.7 NH3What is the isoelectric point of this tripeptide?

Peptides are composed of amino acids. Some amino acids have ionizable side chains while others do…

Answered: The structure below shows a tripeptide…

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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A mixture of proteins contains four different polypeptides, all in ~equal concentration, in solution with the following properties: Protein Molecular Mass (kDa) Isoelectric point A 45 4.5 B 77 6.0 C 28 4.1 D 14 10.7 A fraction of the protein solution is applied to a strong cation exchange column using a buffer at pH 8.0 with increasing [NaCl] from 0.05 M – 1.0 M. The chromatogram is shown below: 1. Based on the data presented, which of the following statements is true: Peak #1 is protein D Peak #4 is protein C Peak #3 is protein A Peak #4 is protein D Peak #2 is protein B 2. Since you know that the proteins are all present in approximately equal concentrations, the different relative peak areas tell you that: There are more neutral amino acids in protein #4…
Which of these compounds is most soluble in water at pH 7.0? (Note that the non- ionized forms are shown, and remember that ionization will impact solubility!) ( CH3-CH2-CH2-CH2-NH2 CH3-CH₂-CH₂-CH₂-CH3 O CH3-CH2-CH2-CH2-CHO OCH3-CH₂-HCO-O-CH3 (an ester)
Some phospholipid species can be phosphorylated beyond the phosphate attached to the #3carbon. Describe the likely structure of such a phospholipid.Would the mass / charge (m/z) ratio of this molecular increase or decrease upon modification?
Polymer beads (resin) made of DEAE (diethylaminoethyl) cellulose are packed in an ion exchange column. The total mass of beads in the column is 8.47 kg. On average, each bead weighs 0.0023 g and has an average of 18.4 * 10° positively charged amine groups that can adsorba negatively charged protein that passes through the column. A solution containing 2.07 mg/L of a protein is maintained at pH 6.3 and is passed through the ion exchange column at 0.215 L/min. The protein has a molecular weight of 154,000. The pk, of the amino groups on DEAE cellulose is 7.1, and the pl of the protein is 5.6. 2. A. How long can the column be operated before reaching 80% capacity (i.e., 80% of the amino groups on DEAE are bound to the protein through an ionic bond)? You may assume that one protein attaches to one + charge on the beads (although it's possible that proteins attach to more than one + charge). B. After reaching 80% capacity, explain what you would do to release the protein attached to the…
Draw dipeptide Arg-Thr at pH 6.0. Circle the six atoms that are restricted in one plane. Calculate its approximate pI assuming pKa for NH3+ is 10.0, pKa for COOH is 3.0, PKR for Arg is 12.0
What is the net charge of the following amino acids (A, B, C, D) at pH 5.96 ? Amino acid Isoelectric point Net charge at pH 5.25 A. 10.76 O+1 00 O-1 B 7.59 O+1 00 O-1 3.00 O+1 00 O-1 5.96 O+1 00 0-1
AH = - 1.2 kcal/mol; Кр 3 16 nM OH 1 HO AH = - 6.0 kcal/mol; Kp = 76 nM OH HOll AH = - 5.5 kcal/mol; Kp = 0.5 nM OH 3 (iv) Consider the molecule 1 being derivatized to yield molecule 2. How would you expect AG for the binding process (to their target) of 2 to compare to 1? Justify your answer.
Which of the following statements concerning the titration curve of glycine is correct? 2.0 E 1.5 1.0 0.5 B 4 6 8 10 pH Point C represents the region where the net charge on glycine is zero. Point D represents the pK of glycine's carboxyl group. Point E represents the pl for glycine. Point A represents the region where glycine is deprotonated. Point B represents a region of minimal buffering. Equivalents OH added
Mixtures 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 alanine
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The oligopeptide GEHRKDYWCM was isolated from blood plasma. Calculate its net charge to the nearest 0.01 at pH 7.6. Show all calculations

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The structure below shows a tripeptide at physiological pH with the protonatable groups labeled with their corresponding oka's. B pka-10 H₂N pKa -3.7 Ö What is the isoelectric point of this tripeptide? pka-4.1 E pka-10.7 NH3 pka -2