Draw the two amino acids serine and alanine, and a dipeptide that could be formed by combiningthese two amino acids (ala-ser). Draw these molecules at a pH=7. In peptide nomenclature theamino terminus is on the left and the carboxyl terminus is on the right.1. How many waters were released by formation of this dipeptide from individual amino acids?[ Select ]2. How many hydrogen bond donors does your dipeptide have? [ Select ]3. If you were to draw this dipeptide at a pH:1, would the number of hydrogen bond donorschange? [ Select ]

Amino acids are the building blocks of proteins which are composed of amino group (NH3+), carboxyl…

Answered: Draw the two amino acids serine and…

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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Consider a protein in which a negatively charged glutamic acid side chain (pKa=4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa=6.5). Part C: Justify your answer with calculations of partial charges on these amino acid side chains at pH=7.9.(Hint: Consider lessons from Coulomb's law, and the Henderson-Hasselbalch equation.)
What are the charges of the following amino acids peptides at ph 14? 1. GLAVV 2. RRKKQ
You will now build a 15 amino acid peptide using another paper or wire backbone as you did above. You will pick 15 amino acids, matching the criteria below, and put them onto your backbone about 3 inches apart. This will be the primary structure of your novel protein. Select 15 amino acids that meet the following criteria 6 hydrophobic R groups 2 acidic R groups 2 basic R groups 2 cysteine R groups 3 hydrophilic R groups Place the R groups in any order you choose on your paper or wire backbone as you did above. Start at the N-terminus and place each R group about 3 inches apart until all 15 are attached to the mini toolbar. You have just built the primary structure of your protein. Question 1: Record the sequence of amino acids in your protein, starting with the N-terminus. The N-terminus is the end of the polypeptide that has a free nitrogen group. The C-terminus, or carboxyl end, will have a free carboxyl group. You can use the three letter amino acid abbreviation to…
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
Draw the structural formula of the oligopeptide if the amino acids are arginine, glutamine, glycine, methionine and glutamic acid considering the first amino acid is the N-terminus
1. Draw the tetrapeptide Met-Ala-Thr-Thr at a ph of 7? 2. Draw the tetrapeptide Met-Ala-Thr-Thr at a ph of 12?
A cytosolic protein has an important alpha amino group. The pKa of this group is approximately 8 when exposed to water outside of a protein. 1. What would happen to the pKa if this group was instead buried in the hydrophobic interior of the protein? Explain. 2. Let’s say in the hydrophobic interior of the protein, the group forms an ionic bond with a carboxylate group of the side chain of a charged Asparagine residue. How would the pKa of this alpha amino group compare with the pKa of the alpha amino group in the hydrophobic interior of the protein without a nearby Asparagine residue to form this ionic bond? Explain.
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?
Regarding the last answer choice, how come both alpha helices and beta sheets aren't denatured when the heat breaks peptide bonds? If heat were to break peptide bonds, wouldn't that affect the primary structure which inevitably affects the more complicated structures?
please match all of them
Glutamine is an amino acid that has -CH₂-CH2-CO-NH₂ as its R group. The R group of the amino acid isoleucine is -CH2-CH-(CH3)2. If these amino acids were in a globular protein in aqueous solution, where would they most likely be? O Both glutamine and isoleucine would be in the interior and on the exterior of the globular protein. O Glutamine would be in the interior, and isoleucine would be on the exterior of the globular protein. O There isn't enough information O Both glutamine and isoleucine would be on the exterior of the globular protein. O Isoleucine would be in the interior, and glutamine would be on the exterior of the globular protein.
Can you please explain how to solve this problem?

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