25) Below are two amino acids: cysteine and histidine. a) Draw the reaction mechanism of a dehydration synthesis reaction between cysteine and histidine below: HS je os OH HN H 'Н 'OH
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- 25) Below are two amino acids: cysteine and histidine. a) Draw the reaction mechanism of a dehydration synthesis reaction between cysteine and histidine below: HS H Product 1 N OH HN H b) Draw two different products of the dehydration synthesis reaction from part a). Prove that these are two different products by labelling the N and C termini, peptide bond, and R-groups of each product. Product 2 OH1. Amino acid analysis of the peptide gave the following residues: Asp Met The following facts were observed: a) Trypsin treatment had no effect. b) The phenylthiohydantoin released by Edman degradation was Leu Lys Phe Tyr What is the amino acid sequence for this heptapeptide? H C-C-CH₂ H c) Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. d) Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys.1. The R group of the amino acid lysine is: -CH2-CH2-CH2-CH2-NH2. Draw the structure of lysine, including the sites of ionization, under the following conditions: 16 NI a) strongly acidic solution; b) neutral solution; c) strongly basic solution Drifed them ard What are the results of the following test on lysine? c) nitroprusside a) ninhydrin; b) biuret;
- a) From the chemical structure above, write the amino acid sequence using both three-letter and one-letter abbreviations. Disregard chirality for this question. b) Indicate adjacent to the alpha-carbon of each residue whether it has an L- or D-configuration.Select the term in column B which best matches the description in column A. There are more terms then needed. Column A Column B 1. The pentose sugar found in DNA. a) Cis fatty acid b) Trans fatty acid c) Coenzyme d) Cofacipr 2. Commonly referred to as "insoluble fiber". 3. Considered to be an amphipathic molecule. 4. A molecule with the formula C18H3602 is probably a e) Phospholipid 5. Bond created during the formation of the primary structure of a protein. ) Glycogen 6. A non-protein organic molecule needed for proper enzyme functioning. g) Cellulose 7. Pyrimidine base found only in RNA. h) Galactose i) Fructose 8. Increasing the number of these molecules in the cell membrane would increase the permeability of the cell membrane. i) Thymine k) Uracil 9. Bond which connects nucleotide monomers together. 1) Fatty acid m) Disaccharide n) Peptide bond o) A-Helix p) B-Pleated Sheet q) Ribose r) Deoxyribose 10.Let’s consider histidine as a free amino acid in aqueous solution. a) Draw the most likely structure of histidine under biochemical standard state conditions. b) Given that free histidine has the following three pKa values, assign each to its corresponding acidic hydrogen or conjugate base in your structure from part a). pKa1 = 1.7; pKa2 = 6.2; and pKa3 = 9.1 c) For each pKa, give the corresponding expression for the equilibrium constant. It helps to write out the chemical equation for each. d) Create a speciation diagram for histidine by plotting Xi vs pH from pH = 4 to pH = 8 where Xi is the mole fraction of the two histidine species involved in the K2 equilibrium in part c).
- Draw the potential tautomers of guanine. (ii) Based on Question 1c) (i), label the patterns of hydrogen bond acceptors, donors and non-polar atoms/groups in the minor groove of the GT base pair.When polynucleotides are synthesized with repeating triplets of nucleotideresidues, one, two, or three different polypeptide chains will be produced incell-free synthesis.(a) Explain why these different results are possible.(b) Predict polypeptides produced when the following are used with anE. coli system: (GUA)n, (UUA)n.(a) A decapeptide has the following amino acid composition: Alaz, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides: Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly. Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine om the experimental data, deduce the primary structure of the decapeptide.
- There is parts A-D for the picture provided. A) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 1? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 B) A peptide has the sequence Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 5? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 C) Same Peptide sequence, What is the net charge at pH8.5, (N-terminus is pronated) Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 D) A peptide has the sequence, Arg-Cys-His-Tyr-Glu-Asn-Lys-Asp. What is the net charge at pH 13? Choices: -5 -4 -3 -2 -1 0 +1 +2 +3 +4 +5 Thank You!Polypeptide Handout Amino acids are linked together to form a peptide bond through an aminidation reaction. The-COO group of one amino acid reacts with the -NH3+ of another amino acid. When two are more amino acids are linked together a peptide is formed. Draw the Following Polypeptides: a) Gly-Ser-Met-Lys b) Lys-Pro-Val-His c) Trp-Thr-Leu-lle d) Cys-Met-Phe-Glu e) G-L-A-R-E f) G-L-A-D g) F-H-E-D h) K-E-M-SWrite out the structures for the cofactors involved in the following biochemical reactions: a) Methylation. b) Amino acid decarboxylation. c) A Claisen reaction. d) Ketoacid decarboxylation. e) Aldehyde reduction s ils otvteimaoomate nglaas bns vilanebl (d ienoiamlalblos tom orls ylianabl (o uencioiqeb of ezed aldstiua s jang2 (b adullb diiw aem (OatHer) nihshsw ( otsibammi dainiw (OatHer) 1aubong wan alobizobyrd moiboe ordt nadw owxim