3 SAQ: Consider the structure (at physiological pH 74) of the following molecules and then answer the questions below.Valine, Leucine, Isoleucine, Lysine1. What is the charge of each of these amino acids at pH 74 and why? Explain by describing the properties of ecach functional group within the molecules:2. One of these molecules has a key structural difference, relative to the others. Name the molecule that is the 'odd one out' and describe the key structural difference.

Amino acids are made up of a central carbon attached to a hydrogen atom, an alpha-amino group, an…

Answered: SAQ Consider the structure (at…

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section3.1: Carbon Atoms And Organic Molecules

Problem 3C

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a. what general category would you place this molecule in of the four categories of biomolecules? b. List 5 functional groups you see in this molecule?
b. Please draw the structure of the polypeptide: threonine-lysine-glutamine-valine at pH 7.0, and identify the alpha carbons. C. Estimate the isoelectric point of the polypeptide in (b.)?
Amino acid structure and composition: Assuming physiological pH conditions, draw the peptide backbone of a protein composed of four amino acids. The protein is a) overall positively charged b) capable of forming disulfide bond with another protein c) has two amino acid that can participate in hydrogen bond formation d) one peptide bond in cis conformation you must show the complete name, single letter abbreviation and structure of each amino acid. Make sure to highlight the peptide bond that is in cis conformation
A/B: 3. Amino acid residues and peptide bonds (a) Draw the chemical structure of F, S and H joined by peptide bonds and also connected to neighboring residues as found in a protein. (b) Include all charges as expected at physiological pH (pH = 7.5) () Rank these three amino acid residues by hydrophobicity, pKa, and by nucleophilicity (d) For the central amino acid residue, identify the phi and psi dihedral angles by drawing a curved arrow indicating rotation about the chemical bond. (e) What group(s) eclipse each other if Phi = 0 degrees? Words and Pictures. (f) While Phi = 0 is not well tolerated, Psi = 0 is not uncommon, a so-called “allowed" but not most-favored region of the Ramachandran plot. What group(s) eclipse each other if Psi = 0 degrees and why is this less problematic than the situation created by Phi = 0. Words and Pictures H₂N* Pka: 9.13 H₂C с C._hydrophobicity: 1. phenylalanine (most) 2. Serine 3. Histidinelleast) ده H H. HIN OH I CH₂ CHO pka: 1. Serine (nighest) 2.…
Activity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1. Glycyl-valyl-serine 2. Threonyl-cysteine 3. Isoleucyl-methionyl-aspartate
D. Draw the structure of Histidine and Imidazole. Why do you think we use Imidazole to elute the protein? Why do we use a 6X His tag?
A. Consider the dipeptideVal–Pro: What amino acid is the N terminal aminoacid? What amino acid is the C terminal aminoacid? How are the amino acids connected? Give the name of the dipeptide. Give the name of the dipeptide in which the amino acid order is reversed as Pro–Val.
pls answer the following question. -Which amino acids contain the following?a.sulfur/sulfhydryl group b. aromatic group c. imidazole ring d. guanidine group e. indole group -Classify the following proteins according to their biological function: casein, albumin gluten, and myoglobin. -Which levels of protein structure organization are lost during hydrolysis and denaturation? -What is the Beer-Lambert's Law? Why is it relevant to the quantitative analysis of proteins? -What are the other protein components of milk aside from casein?
a. Suppose that the R group of a histidine residue in a protein in its native tertiary structure is buried in the interior of the protein and is involved in a salt bridge (ionic interaction) with an oppositely charged residue. Unfolding the protein exposes both of the charged groups to water. Would you expect the pKa of the His R group (side chain) in the native protein to be a) higher or b) lower than the pKa of the same residue in the unfolded protein? Why? b. Is the exocyclic NH2 in cytosine acidic or basic? Why? NH, `N'
Provide the simIlarities and differences of different functional groups of amino acids? Explain thoroughly
Activity: Write the line structure of each of the following peptide at pH7 and identify how many peptide bond in each number. 1 Alanyl-phenylalanine 2. Lysyl-alanine 3.Phenylalanyl-tyrosyl-leucine
What are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved. The molecule considered is a protein: pancreatic amylase.

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