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- 1. Draw the structural formula of the amino acid valine that predominates in solution at each of the following pH values. А. рH 3D7.0 В. рH %3D 12.0 С. рH %3D 2.0 2. Draw the structural formula of the amino acid phenylalanine that predominates in solution at each of the following pH values. А. рH%3D 3.0 В. рH %3D 10.0 С. рH%3D 7.0In ion-exchange chromatography, amino acids are separated on the basis of electro-static interactions and hydrophobic interactions with the resin. The chemical structure of the resin pol-ymer with a negatively charged sulfonic acid group is shown to the right. An elution profile for the aminoacids using this resin is given below. Based on the elution profile above, explain the following:Draw the amino acid product that results from a transamination reaction involving pyruvate and glutamate, shown in the image below. Draw the product as it would occur at the pH of most body fluids, including all charges. You do not need to draw the other product of the reaction. O NH3 3D CH3-C-C-o-+ 0-CH-CH CH2-C-0--→? pyruvate glutamate Draw the molecule on the canvas by choosing buttons from the Tools (for bonds), Atoms, and Advanced Template toolbars. The single bond is active by default. Include all hydrogen atoms and charges. > View Available Hint(s) CONT. H. N. NV CI Br 1] -C- C1 SI
- Which of these heterocyclic drugs is likely to be the least soluble in water? Use the Fsp³ parameter to decide. OH Tramadol Chemical Formula: C16H25NO2 YOUR OW Pantoprazole Torasemide Chemical Formula: C16H15F2N3O4S Chemical Formula: C16H20N4O3S Temazepam -OH Chemical Formula: C16H13CIN₂O2 Tioconazole Chemical Formula: C16H13C3N₂OS A. Tramadol B. Pantoprazole C. Torasemide D. Temazepam E. Toconazole4. A solution containing egg albumin (pl-4.6), B-lactoglobulin (pl-5.2), and chymotrypsinogen (pl=9.5) was loaded onto a column of diethylaminoethyl cellulose (DEAE-cellulose) at pH 5.4.The column was then eluted with a pH 5.4 buffer, with an increasing salt concentration. Predict the elution pattern.Determine the Primary amino acid sequence of an Octapeptide Composition · Tyr , Arg,Pro, Lys ,Lys ,Met ,Trp,Phe N terminal 1 2 3 4 5 6 7 8 C terminal 1) Treatment with an Edman reagent gives a PTH-AA that shows a Yellow color with Ninhydrin. 2) Trypsin digestion of the Octapeptide gives tetepeptide, dipeptide, free Arg ,free Trp. 3)CNBr = pentapeptide and tripeptide. 4) chymotrysin - tetapeptide and two dipeptiele. The tetrapeptide contains an amino acid with an OH group in the side chain.
- Chitinase is a protein that breaks down chitin, a primary component of the cell wall in fungi, scales in fish and exoskeletons of arthropods. The activity of chitinase extracted from a plant was shown to be optimum at pH 5. You were tasked to prepare 300 mL of 150 mM buffer solution for further analysis of the extracted chitinase. REAGENTS Ka 2.5M Acetic acid Solid NaOAc•3H2O [136.08g/mol] 1.76 x 10-5 2.5M NH3 Solid NH4Cl [53.49g/mol] 5.6 x 10-10 2.5M Lactic acid Solid sodium lactate [112.06g/mol] 4.0 x 10-5 5 M HCl 5M NaOH Pls show sol'ns 1. Given the following reagents, give the moles of each component (acid & base).2. What are the mass/volume of the components needed to prepare the buffer? 3. What will the pH of the buffer be if 1mL of 5 M NaOH was added?A 100 mL solution of 0.1 M glycine at pH 1.72 was titrated with 2 M LIOH. The pH was monitored and the result were plotted as shown in the graph. The key points of the titration are designated as I to V. Identify the key point in the titration corresponding to the pH at which the carboxyl group is half deprotonated. 12 JL30 (V) 9.60 (IV) 8 5.97 pH 6 2.34 CII) 2 (I) 0.5 1.0 1.5 2.0 OH (equivalents) IV O Il and IV Nextcomplete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.
- 1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex SeriosThe 3 proteins have the following properties. Which is the correct order of steps to extract them? + ethyl acetate, + (NH4)2SO4 at 20% saturation, centrifugation, + detergent (Triton X), buffer the lysate (pH=10), centrifugation, collect precipitate + ethyl acetate, + detergent (Triton X), + (NH4)2SO4 at 20% saturation, centrifugation, buffer the lysate (pH=10), centrifugation, collect precipitate + 1 M NaCl, + detergent (sodium dodecyI suIfate), centrifugation, +(NH4)2SO4 at 60% saturation, buffer at pH 7, centrifugation, collect precipitate + ethyl acetate, adjust pH to 7.3, centrifugation, collect supernate, +detergent (Triton X) to precipitate, +(NH4)2SO4 at 30% saturation, centrifugation, collect precipitate1. 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.