2. Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, pleaseshow in zig-zag style, from amino to carboxy terminus, with correct stereochemistrya. Draw the predominant form at pH = 2b. Draw the predominant form at pH = 5c. Draw the predominant form at pH = 7d. Draw the predominant form at pH = 12

Recall that:Amino acid sequences are written with N-terminal amino acid on the left and C-terminal…

Answered: 2. Consider the peptide…

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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Amino acid sequence in a protein that can form N-glycosylation is called a glycosylation sequon. Which of the following is such a sequon? a. Asn-Ala-Thr b. Gln-Ala-Thr c. Asn-Pro-Pro d. Asn-Ala-Ala e. Gln-Ala-Ala
Draw the L enantiomer in a Fischer projection for each amino acid; identify the amino acid as neutral, acidic, or basic. Give the three-letter sign [3], and the one-letter symbol [4].arginine a. arginine b. arginine c. a. glutamic acid b. glutamic acid c. glutamic acidtyrosine b. valine c. arginine
please help in under 30 mins
Patients suffering from sickle cell anemia have a mutation in the gene that codes for one of the hemoglobin chains, in which a single glutamate is replaced by a valine. Propose an explanation for why this substitution has such a striking effect on protein structure and function with explanation. Suggest two other amino acids that would be less likely to cause such serious impairment of hemoglobin function if each was substituted for glutamate. Briefly explain your answer.
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
1. Sickle cell anemia results from a substitution of a valine for a glutamic acid. What do you expect the effect might be if the mutation were to have placed a leucine at that site? An aspartic acid? 2. Of the following amino acids, glycine, isoleucine, and lysine, which would you expect to be the most soluble in an acidic aqueous solution? Which the least? 3. How many structural isomers could be formed from a molecule with the formula C5H12? C4H8?
please match all of them
A. Where would you expect valine, leucine, and isoleucine to be located in a polypeptide? (Inside or outside)? Explain your answer using the properties of the amino acids listed. B.How would your answer change, if the amino acids were Lysine and Histidine?
What is glycogenesis? What are the different enzymes involved and the specific catalysis reactions in glycogenesis? What are the important products in glycogenesis? please answer all
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).
At what pH can you separate the following peptides: ala-ala-ala, glu-glu-glu, his-his-his? OA 2.0 B. 4.0 C. 5.0 O D. 7.0 E. 9.5
You are analyzing the peptide ala-ile-glu-lys-phe-val- tyr-cys. If you treat the peptide with chymotrypsin, which technique would be best to separate the fragments? O a. ultracentrifugation O b. affinity chromatography O c. dialysis d. gel filtration chromatography O e. ion exchange chromatography What is an advantage of NMR spectroscopy over x-ray crystallography in studying protein structure?

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