GT 2A. Draw the structure of L-valine in a strongly basic solution.B. What is the charge of this amino acid in a strongly basic solution?1.2. A. What is the pH of D at its isoelectric point?B. Show the structure of this amino acid at its isoelectric point.C. What is the charge of this amino acid in a strongly acidic solution?

A. Structure of L-valine in a strongly basic solution is as follows: B. The charge of this amino…

Answered: A. Draw the structure of L-valine in a…

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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4. Let’s build a polypeptide chain a. Using your arsenal of 4 amino acids, write out the primary structure of an 8 amino acid long polypeptide that you might be called amphipathic and thus allow it to form a micelle in aqueous solution, identify amino acid 1 through 8 as well as the location of the amino and carboxy termini of the polypeptide. b. Explain why this polypeptide would be considered amphipathic and draw what the micelle might look like in water. c. Taking amino acids 3, 4, and 5, draw the molecular structure of this particular stretch of polypeptide chain. Along the backbone linkage of the polypeptide identify the peptide bonds with a PB, the bonds with free rotation FR, and bonds with limited rotation LR.
a. What is a heterocyclic amine? What was the most interesting example you found out about? Why was it interesting? b. DNA and RNA are heterocyclic amines with Nitrogen in the center. If sulfur were in the middle of the ring instead of Nitrogen how would this affect the ability to H-bond? c. Show the structure of 2 neurotransmitters. What are some of the interactions you found out about it.
5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0
Dinah had her curly hair rebonded. One chemical is put on her hair to break the disulfide bonds that give the hair stands their shape (curly) and a second chemical is used to reform the disulfide bonds to hold the hair in a straight position. a. What level(s) of protein structure is/are affected by these processes? b. Why doesn’t the hair stay straight forever after this treatment
Can you please explain how to solve this problem?
a. which amino acid can form a covalent bond with its side chain? b. which amino acid can contribute to protein tertiary and quarternary structure by forming a covalent bond?
The side chain of acetyl-L-lysine-OMe has a pKa=10.5 and its acid-dissociation reaction is shown below. see attachment for Question D.
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
provide detailed explanation.
For the tetrapeptide KASE: a. Draw its complete protonic equilibria. Indicate the net charge of each form and encircle the zwitterionic form. b. Give the full name of the tetrapeptide. c. Calculate its IpH. d. If the tetrapeptide was subjected to electrophoresis using a buffer solution at pH 7, at which electrode it will migrate?
Match amino Acid R group characteristics to the biochemical bond it can form. Alanine ◆ Glycine Proline Aspartic Acid Lysine Tryptophan ◆ Methionine Threonine Asparagine Histidine A. Pi-bonding aromatic bonds B. Non-polar, contains a sulfur atom C. Non polar bonds D. Amide group bonds E. Inserts a kink (non-freely rotating bond F. Anionic group donating bonds G. Hydroxy group bonding H. Cationic group with pK = 6.0 I. No-R group - highly flexible J. Cationic group donating bond
Shown is the electrophoretic profile of a pure protein ran at different pH values HH (+) (-) pH 5 pH 6.5 pH 7.4 pH 9.2 What is most likely the reason for the change in the position of the protein band at pH 9.2? A. deprotonation of internally located basic amino acid residues B. deprotonation of N-terminal amino acid C. deprotonation of an internally located basic amino acid, his D. deprotonation of acidic amino acids, glu and asp E. deprotonation of cys

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