32) You are working with an molecule with a pl of 6.00 and the pKa's of the ionizablegroups on the molecule are 1.3, 4.1 and 7.9. You would like this amino acid tohave a net negative charge. Which of the following pH values would result in a netnegative charge?A) 1.3B) 4.1C) 4.43D) 6.0E) 7.9

● If the pKa is lower than the pH the molecule will be deprotonated i.e it will carry negative…

Answered: 32) You are working with an molecule…

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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1)Ubiquitin is a small protein with a monoisotopic mass of 8560 Da. a) Electrospray ionization of this small protein typically results in major charge states of +8, +9, +10, +11, +12, and +13. Using this information, complete the table below, assuming the charges on each come from protonation. Report mass and m/z values to the ones place. b) Using the data you entered in the table, sketch an expected ESI-MS spectrum for ubiquitin. Label each peak with its charge state. What do you notice about the spacing of peaks along the x-axis. c)The figure shows an experimentally obtained electrospray mass spectrum for ubiquitin. Compare this spectrum to the spectrum you predicted. Are there any differences? If so, what might cause these differences?
a) Draw a non-covalent interaction between a water molecule and the charge on a phosphorylated serine residue(not including backbone atoms). What type of interactuon is this, how strong is it, and what holds the interaction together? b)Draw a non-covalent interaction between an alanine residue and a valine residue(not including backbone atoms). What type of interaction is this, how strong is it, and what holds the interaction together?
A mixture of Alanine (pl 6.02), Glutamic Acid (pl 3.22), Glycine (pl 5.79), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2 ? v First 1. Alanine v Second 2. Glutamic Acid v Third 3. Glycine v Fourth 4. Lysine v Fifth 5. Threonine 6. No separation
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
Consider an amino acid (A) with no ionizable side chains, and call the three species involved in the acid/base equilibria H2A+, HA, and A- (see scheme below). Assume that pKa(1) = 2.0 and that pKa(2) = 9.0. Suppose that the total concentration of the amino acid is 1.0 mM. Report to two significant digits. pH [H2A+] (mM) [HA] (mM) [A-] (mM) 1.0 2.0 3.0 4.0 5.0 6.0 7.0 8.0 9.0 10.0 11.0 12.0
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 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)
A 100 ml solution of 0.1 M amino acid (AA) at ph 1.0 was titrated with NaOH solution. The pH was monitored, and the results were plotted on the graph. The keypoints in the titration are designated I to VII. What is the possible identity of the amino acid? What is the isoelectric point of AA? what is the pKa corresponding to the dissociation of the alpha carboxylic group? Region/point where AA is predominantly present as a (-1) charged species? The effective buffering range for the amino acid in the acidic region? Region/point where the solution has 50:50 percent mixture of the (0) and (-1) species
You are given 0.5 M solution of the amino acid Arginine. pK1 (α-carboxyl group) = 2.17 pK2 (α- amino group) = 9.03 and pK3 (guanidine group) = 12.48 Determine the pH of the solution if you add 15 mL 0.25 M HCl to 10 mL of the 0.5 M Arginine. Assume that Arginine is in isotonic state. Show all calculations b. Draw the structure of the amino acid at the pH determined in question 1
You are given 0.5 M solution of the amino acid Arginine. pK1 (α-carboxyl group) = 2.17 pK2 (α- amino group) = 9.03 and pK3 (guanidine group) = 12.48 Determine the pH of the solution if you add 15 mL 0.25 M HCl to 10 mL of the 0.5 M Arginine. Assume that Arginine is in isotonic state. Show all calculations
The following amino acid is dissolved in solution at pH 7.4. HC H' + CH CH₂ H/ H+ HC a. Which amino acid is this? (all lower case) N- H CH CH₂ b. What is the pKa of its ionizable side chain? (Use the value from the textbook.) c. What is the ratio of the uncharged to the charged form at pH 7.4? (write answer as number with one decimal place, ex 2.5 or 0.2 or 50.0 with an implicit "to 1")
At pH 7.0, in what order would the following three peptides (described by their amino acid composition) be eluted from a column filled with a cationexchange polymer?Peptide A: Ala 10%, Glu 5%, Ser 5%, Leu 10%, Arg 10%, His 5%, Ile 10%, Phe 5%, Tyr 5%, Lys 10%, Gly 10%, Pro 5%, and Trp 10%.Peptide B: Ala 5%, Val 5%, Gly 10%, Asp 5%, Leu 5%, Arg 5%, Ile 5%, Phe 5%, Tyr 5%, Lys 5%, Trp 5%, Ser 5%, Thr 5%, Glu 5%, Asn 5%, Pro 10%, Met 5%, and Cys 5%.Peptide C: Ala 10%, Glu 10%, Gly 5%, Leu 5%, Asp 10%, Arg 5%, Met 5%, Cys 5%, Tyr 5%, Phe 5%, His 5%, Val 5%, Pro 5%, Thr 5%, Ser 5%, Asn 5%, and Gln 5%

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