Steps 1 & l': Transimination: Enzyme Enzyme H Enzyme R-C-CO0 H-N (CH2)4 (CH)4 (CH)4 H H-C H H- NH H-C R- -COO + NH, 2-0, PO 20,PO CH3 CH3 CH H Amino acid-PLP Sehiff base (aldimine) a-Amino acid Enzyme-PLP Schiff base Geminal diamine intermediate Steps 2 & 2': Tautomerization: Lyn-Enzyme Lys - Enzyme Lys-Enzyme COH H,N: R- C00 H,NH R-Ça C00 H,NH R-Ça-CO0 H-C H-C 10,PO CH3 CH, CH Ketimine Resonance-stabilized intermediate Steps 3 & 3': Hydrolysis: Lyn-Enzyme Lys - Enzyme H. H,N: H,N: R-C-CO0 H-C-H NH H-C-H 2-0, PO R--CO0 a-Keto acid 20, PO CH CH Pyridoxamine phosphate (PMP)- Carbinolamine enzyme

Steps 1 & l': Transimination: Enzyme Enzyme H Enzyme R-C-CO0 H-N (CH2)4 (CH)4 (CH)4 H H-C H H- NH H-C R- -COO + NH, 2-0, PO 20,PO CH3 CH3 CH H Amino acid-PLP Sehiff base (aldimine) a-Amino acid Enzyme-PLP Schiff base Geminal diamine intermediate Steps 2 & 2': Tautomerization: Lyn-Enzyme Lys - Enzyme Lys-Enzyme COH H,N: R- C00 H,NH R-Ça C00 H,NH R-Ça-CO0 H-C H-C 10,PO CH3 CH, CH Ketimine Resonance-stabilized intermediate Steps 3 & 3': Hydrolysis: Lyn-Enzyme Lys - Enzyme H. H,N: H,N: R-C-CO0 H-C-H NH H-C-H 2-0, PO R--CO0 a-Keto acid 20, PO CH CH Pyridoxamine phosphate (PMP)- Carbinolamine enzyme

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter16: Gene Expression

Section: Chapter Questions

Problem 3VCQ: Figure 16.13 An increase in phosphorylation levels of elF-2 has been observed in patients with...

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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.
Figure 16.13 An increase in phosphorylation levels of elF-2 has been observed in patients with neurodegenerative diseases such as Alzheimer’s, Parkinson's, and Huntington's. What impact do you think this might have on protein synthesis?
Given the peptide Val-Ser-Gln-Lys The lateral chain of one of these amino acids can be modified by N-acetylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7 The lateral chain of one of these amino acids can be modified by phosphorylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7.
if the reaction pH drops significantly (pH=2 for example), how would reaction catalyzed be serine proteases be affected? why? (assumin that the rest of the protein structure remain intact)
1. Consider the following α helix from myoglobin at pH 7. Gln-Gly-Ala-Met-Asn-Lys-Ala-Leu-Glu-His-Phe-Arg-Lys-Asp-Ile-Ala-Ala-Lys-Tyr(a) Label amino acids in the polypeptide above as follows: p for polar and uncharged, np for non polar, – for negatively charged, and + for positively charged.(b) How many complete turns are there in this helix?(b) Which side chains are likely to be on the side of the helix that faces the aqueous solvent? Why?(c) Which side chains are likely to face the interior of the protein? Why?
Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide.
Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide. I don't understand how the order of amino acids in Step 2 was arranged. Please explain. Thank you.
Amino sequence: Gln-Glu-Val-Leu-Ile-Arg-Leu-Phe-Lys-Gly-His-Pro-Glu-Thr-Leu-Glu-Lys-Phe-Asp-Lys-Phe-Lys-His-Leu-Lys-Ser-Glu-Asp-Glu-Met-Lys-Ala-Ser-Glu-Asp-Leu-Lys A) List the fragments generated with trypsin: B) List the fragments generated with chymotrypsin (5 pts) (assume reaction conditions are used to maximize cutting to the C-terminal size of only the 3 aromatic amino acids.)
don't copy 6. A protein-ligand binding reaction is run. At equilibrium, half the protein is ligand bound, the unboundligand concentration is 0.657 nM. Calculate the koff value for this reaction. Assume the kon value is typical ofprotein-ligand interactions.
Legend: Blue – wild-type β-galactosidase Red – mutant β-galactosidase _________ a. What is the optimum pH of wild type β-galactosidase? _________ b. What is the optimum temperature of mutant β-galactosidase? _________ c. Which enzyme has the greater activity at pH 7.2? _________ d. Which enzyme has the greater activity at a temperature of 42.5oC? _________ e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? _________ f. Which enzyme has greater activity if temperature increases from 40oC to 41 oC?
DO NOT COPY OLDER ANSWERS! AND SHOW FULL WORK! I have a mixture of 4 proteins, whose sequences are shown below (note that each protein is a 100-repeat of the sequence shown). Protein A: (Gly-Ala-Lys-Val-Ile-Phe-Glu-Val-Asn-Gly) Protein B: (Ala-Ala-Lys-Arg-Ile-His-Glu-Ala-Asn-Lys) Protein C: (Glu-Val-His-Asp-Ala-Asp-Glu-Val-Asn-Asp) Protein D: (Ala-Lys-Arg-Phe-Trp-Phe-Gly-Ile-Ala-Gly) 1) Which protein/s are MOST LIKELY to precipitate out at a pH of 3.5? a) A b) B c) C d) D e) B & C f) A & D g) None of them h) Cannot be determined.
Deduce the amino acid sequence of a polypeptide from the following:1. Acid hydrolysis gives Ala2, Arg, Lys2, Met, Phe, Ser22. Carboxypeptidase gives Ala3. Trypsin digestion gives 4 peptides a) Ala, Arg b) Lys, Phe, Ser c) Lys d) Ala, Met, Ser4. CNBr treatment gives a) Ala, Arg, Lys2, homoserine, Phe, Ser b) Ala, Ser5. Thermolysin is a protease that cuts on the N-terminal side of hydrophobic amino acids (substrate preference is Leu, Ile, Phe, Trp, Tyr, Val). Thermolysin treatment of our polypeptide yields 2 peptides a) Ala, Arg, Ser b) Ala, Lys2, Met, Phe, Ser