solve a engineer the maltose bindingprotein (MBP) to bind 1, 3, 5 Trinitrobenzene (TNB) - a molecule that is even moreexplosive than TNT! Instead of its natural ligand, maltose, you hope to develop yourmutant into a biosensor that can be used to detect the presence of land mines throughidentification of TNB in the soil.NO₂CH₂OHCH₂OHонA seOHOHNO₂OHOHMaltoseTNBOHAfter the laborious process of mutating the active site of MBP to bind TNB, you identifyfour variants of MBP that bind to TNB with the following affinities:TNB-binding MBP variantABсDKo (μM)8509,0000.430The maximal concentration of TNB that leeches out of land mines into the surroundingsoil reaches only 2 mM (milli-molar). Your advisor asks you to use the Ko values youmeasured to determine which of the variants would be the best candidate for thefollowing purposes. Assume that the fraction of TNB-bound MBP correlates linearly witha signal in your biosensor device from 0 (completely unbound) to 1 (fully bound).a. Which variant would be the most sensitive overall at detecting TNB? Brieflyexplain your answer.

Consider the interaction of a ligand (L) with a protein (P) that leads to the formation of a…

Answered: engineer the maltose binding protein…

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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Shown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CH
During nitrogenous base biosynthesis the C4, C5 and N7 atoms are derived from which amino acid Phenyl alanine Glycine Glutamine Aspartate
A decapeptide which could resist burns was isolated from an endemic plant from Mt. Mayon. Deduce the amino acid sequence of the decapeptide given the following informations. Mercaptoethanol gave two pentapeptides F1 and F2. Chymotrypsin treatment of F1 releases S and a tetrapeptide (C,K,F,M) while F2 gave a dipeptide (M,S) and a tripeptide (C,F,K) F1 when treated with CNBr released a free homoserine lactone and a tetrapeptide. Trypsin treatment of F1 gave a tripeptide and a dipeptide. F2 treated with carboxypeptidase released free M while with trypsin gave free K and a tetrapeptide.
When starved, bacteria produce the intracellular signaling molecule ppGpp (guanosine-3′,5′-bisdiphosphate). Draw its structure.
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Sydney Brennen isolated Salmonella typhimurium mutants that were implicated in the biosynthesis of tryptophan and would not grow on minimal medium supplemented with intermediates in tryptophan biosynthesis, some mutants were able to grow while others remained unable to grow. Review the data attached to order the biosynthetic pathway by both enzymatic step and by intermediate biomolecule. Label the step impacted by each of the mutant cell lines.
The enzyme cytidine deaminase catalyzes the conversion of cytidine to uridine. Cytidine deaminase catalyzes the reaction through an addition of water across the cytidine 3,4-bond, forming a tetrahedral intermediate followed by the elimination of NH3 to form the product uridine. This is like the addition-elimination mechanism that we studied for adenosine deaminase. Cytidine deaminase НО. NH₂ N пOH OH cytosine R + H₂O cytidine The Km value for the substrate cytidine is 2.5 × 10-4 M, and the K; for competitive inhibition by the product uridine is 2.5 × 10-³ M. N R A reduced derivative of the product, 3,4,5,6-tetrahydrouridine was shown to be a fully reversible competitive inhibitor with a Ki of 2.4 x 10-7 M, a value approximately 10,000 times lower than that of the product uridine. NH₂ NH uridine HO. N R R = D-ribose HOH OH uridine 3NH uracil ring numbering H NH H H + NH3 H OH H 3,4,5,6-tetra- hydrouridine a.) Draw a structure of the intermediate that we predict to form during the…
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The bacteria that you are growing to express biochemisfunase are resistant to ampicillin, so you keep ampicillin in your media to prevent contamination from other bacterial strains. You find a tube of ampicillin in the lab freezer that says “2000x AMP” on the lid, which indicates that it is 2000 times more concentrated than what you need (i.e., a concentration of 1x ampicillin in your media). How much of the 2000x ampicillin stock would you add to your 1.0-L culture to get a final concentration of 1x ampicillin?
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