4A. Write out the chemical equations (structures are not necessary) for the two steps inthe reaction catalyzed by aminoacyl tRNA transferase. Include all products andreactants.Step 1: amino acid activationStep 2: aminoacyl transfer to the tRNA4B. Write the chemical equation for the net reaction catalyzed by aminoacyl transferase.This can be determined by taking the sum of the two reactions above.

Amino acyl tRNA synthetase is the enzyme that catalyzes the transfer of amino acid to the specific…

Answered: 4A. Write out the chemical equations…

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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BIOCHEMISTRY. other chegg & bart answer was answered incorrectly. need first blank only Please provide only typed answer solution no handwritten solution needed allowed
E Threonine 6. You have identified some intermediates in threonine synthesis: A, B, C, D and E. You grow a few of your mutants in the presence of these different intermediates to determine the order in which the gene products act. Below are your results. A (+) means growth and a (-) means no growth. Given these data, draw the best possible pathway for the synthesis of threonine. The diagram should use arrows to indicate one intermediate being changed to another intermediate. Indicate which gene produces the product responsible for the conversion by listing the mutant in that gene above the arrow. Mt1 Mt2 Mt4 Mt7
Table 1. Kinetic parameters of a chosen model wild-type (WT) enzyme and three catalytically-improved mutants (M1 to M3). Enzyme variants k (8¹) WT MI M2 M3 50 500 1000 50 K₁, (μM) 10 100 100 1 k/K (HM¹¹ s¹) 5 The study above was done on a wildtype enzyme and three genetically-engineered mutants. The purpose was to find a mutation to improve the catalytic efficiency of the enzyme for industrial use. Which is the most accurate statement concerning the data? M2 is the optimal choice when substrate concentrations are saturating. The wildtype enzyme is still preferable to M3 when S<
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Read very carefully: Chymotrypsin cleaves peptides C TERMINUS to the aromatic amino acids. Trypsin cleaves peptides C TERMINUS to basic amino acids. Cyanogen bromide (CNBR) cleaves C-terminus to methionine residues. With this knowledge, reconstruct the following cleavage products and give the original peptide sequence. CNBR Chymotrypsin WITHHERISALLRIGHT ISTRYWITHM Trypsin EISAM YWITHMEISAMANINGCHEMI STR YWITHHER 1 The which convorted e Name.
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a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
9. Shown below is a binding pocket for a protein with a ligand bound. The ligand interacts with a serine and a valine side chain. ligand a. Briefly explain, in terms of Ka, the effect of a mutation that replaces the serine residue with a valine residue. b. Briefly explain, in terms of Kd, the effect of a mutation that alters the ligand (as seen below) binding to the original, unmutated, binding site. :0: ligand 2
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Small molecules are used as inhibitors of protein action - as drugs. They most often do this by blocking the active site within the protein. Potential drugs can be screened computationally to determine if they are strongly bound to the protein. Figure 1 shows a possible conformation of a candidate drug molecule, 4-bromo-2- carboxymethylamide-pyrrole (abbreviation: BCMAP) at the active site of a protein (abbreviation: PR). Figure 2 shows the full protein structure whilst figure 3 shows a known inhibitor of the protein at the site, overlayed with another calculated conformer of BCMAP. (a) Explain what types of interactions, both intermolecular and intramolecular, that a molecular mechanics forcefield must be able to describe in order to be able to accurately determine the geometry of BCMAP in the protein. Identify which interactions will be the most important to describe accurately. Figure 1.4-bromo-2-carboxymethylamide-pyrrole (BCMAP) (C, N, O, and Br atoms in yellow, blue, red, and…
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