3. Bioconjugate chemistry is a relatively new branch of science wherebybiological macromolecules, sometimes even from different classes, areconnected by a covalent bond or linkage. For example, a lipoprotein ora glycolipid in which part of the molecule is a lipid and part protein oris part carbohydrate and part protein can be considered a bioconjugate,and there are many other examples. After a bioconjugation synthesis,typically medicinal chemists use TLC to determine the extent of theirreaction where it can be used to separate the starting reactants from theproduct (the bioconjugate). For example, consider the reaction of twocysteine amino acids together in the formation of a disulfide bond andthe biological compound cystine (Eq. 3-2):Cys-SH + Cys-SHCys-S-S-Cys (Cystine)Eq. 3-2Draw or sketch what the TLC pattern might look like where thestarting material is separated by the disulfide-bond-linkeddipeptide.

TLC is a versatile and widely used technique in chemistry and biochemistry for separating and…

Answered: cysteine amino acids together in the…

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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Identify the primary structure of a hexapeptide containing five different amino acids if the following smaller peptides are among the partial hydrolysis products: Gly-Cys, Ala-Ser, Ala-Gly, and Cys-Val-Ala
Sketch a titration curve for aspartic acid, andindicate the pKa values of all titratable groups. Also indicate thepH range in which the conjugate acid–base pair +1 Asp and 0 Aspwill act as a buffer
Given below is the name of a polypeptide Valyllysylalanylhistidylaspartylphenylalanylglycylglutamate The average pKas of different groups/side chains are shown in the table below: Group/amino acid side chain pKa C-terminus 3.5 3.9 E 4.1 H 6.0 8.4 Y 10.5 K 10.5 R 12.5 N-terminus 9.0 What is the total charge of this molecule at pH 5? [ Select ] What is the total charge of this molecule at pH 9.5? [ Select] > >
gal(a1→6)gal(a1→6)glc(a1→2B)fru. Which of the complete IUPAC of this tetrasaccharide? a-D-galactopyranosyl-(1→6)-ß-D-galactopyranosyl-(1→6)- a-D-glucopyranosyl-(1→2)-B-fructofuranose a-D-galactopyranosyl-(1→6)- a-D-galactopyranosyl-(1→6)- a-D-glucopyranosyl-(1→2)-ß-fructofuranoside a-D-galactopyranosyl-(1→6)- a-D-galactopyranosyl-(1→6)- a-D-glucopyranosyl-(1<→2)-ß-fructofuranose a-D-galactopyranosyl-(1→6)-B-D-galactopyranosyl-(1→6)- a-D-glucopyranosyl-(1→2)-ß-fructofuranoside
Provide Fischer and Haworth projections for all enantiomers of glucose. Include anomeric forms.
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.
Provide an explanation for the fact that a-D-mannose is more stable than B-D-mannose, whereas the opposite is truc for glucose.
The peptide aspartyl-glutamyl-leucyl-threonyl-alanine, shown in the sketch drawing window, has several ionizable groups. Adjust the charges to show the molecule as it would exist at pH 5.00. Use the pk values in the table below. pK, Values for Ionizable Groups of Amino Acids. Amino Acid pA, of a-COOH pA, of e-NH, pA, of Side Chain Isoelectric Point (pI) Alanine 235 9.87 6.11 Arginine 2.01 9.04 12.48 10.76 Asparagine 2.02 8.80 5.41 Aspartic acid 210 9.82 3.86 298 Cysteine 2.05 10.25 8.00 5.02 Glutzmic acid 2.10 9.47 4.07 3.08 Glutamine 217 9.13 5.65 Glycine 235 9.78 6.06 Histidine 7.11 9.18 6.10 7.64 Isoleucine 232 9.76 6.04 Leucine 233 9.74 6.04 Lysine 218 8.95 10.53 9.74 Methionine 2 28 9.21 5.74 Phenylalanine 2 58 9.24 5.91 Proline 2.00 10.60 6.30 Serine 221 9.15 5.68 Threonine 2.09 9.10 5.60 Trуptophan 238 9.39 5.88 Tyrosine 2 20 9.11 10.07 5.63 Valine 2 29 9.72 6.00 • Use the wedge hash bond tools to indicate stereochemistry where it exists. • If a group is 2chiral, do not use…
Based on the pK, table for amino acids (Table 1.1), draw the structures with net charge, and the equilibria representing the complete deprotonation of aspartate. Table 1.1 Name pK pk2 pKR Glycine Alanine 2.4 9.8 2.3 9.7 Valine 2.3 2.4 9.6 Leucine 9.6 Isoleucine 2.4 9.7 Methionine 2.3 9.2 Phenylalanine Proline Serine 1.8 9.1 2.0 10.6 2.1 9.2 Threonine 2.6 10.4 Cysteine Asparagine Glutamine 1.8 10.8 8.3 2.0 8.8 2.2 9.1 Tyrosine Tryptophan Aspartate Glutamate 2.2 9.1 10.9 2.4 9.4 2.0 2.2 10.0 3.9 9.7 4.3 Histidine 1.8 9.2 6.0 10.8 Lysine Arginine 2.2 9.2 1.8 9.0 12.5
Is serine chiral? Draw serine and identify the chiral atom. Explain why serine is chiral.
Histidine is an amino acid containing an ionizable group in its side chain. This ionizable group has a pka of 6.0, meaning that His is in its deprotonated form at physiological pH (7.0-7.4). However, His is included in the positively charged amino acid category. Calculate the ratio of deprotonated/protonated His at pH 7.0, and use your answer to justify why this amino acid is included in the positively charged amino acid category. Show all work for full credit.

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cysteine amino acids together in the formation of a disulfide bond and the biological compound cystine (Eq. 3-2): Cys-SH + Cys-SH Cys-S-S-Cys (Cystine) Eq. 3-2 Draw or sketch what the TLC pattern might look like where the starting material is separated by the disulfide-bond-linked dipeptide.