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- Which of the following is false regarding Serine Proteases? O They employ general acid-base catalysis They contain a catalytic Triad of His, Ser, and Asp residues They employ metal ion catalysis O They cleave simple organic ester bonds near larger residuesBinding of a ligand to protein X affects the binding properties of another site on X. This is an example of which of the following phenomena? transition state stabilization competitive inhibition noncompetitive inhibition induced fit allosteric regulationUnder what pH conditions can a protein not bind to the beads in a column? pH = -pKa pH = pI pH = 7 pH = pKa In size exclusion/gel filtration chromatography, the elution order is dependent upon Molecular weight Concentration Overall Charge Enzymatic Activity
- Which of the following statement is FALSE ? pKa values of active site residues can be shifted from typical pKa values Enzymes increase Keq Near attack complexes have reacting molecules close enough to form Va der Waals contacts The transition state contains at least one partial bond. QUESTION 12 The angle o in a peptide best describes: O the angle between the two peptide bonds O the angle between the alpha carbon (Ca) and the amide O the angle between the alpha carbon (Ca) and the carbonyl O the angle between the alpha carbon (Ca) and its side chain QUESTION 13 Investigating how protein subunits come together studies: super- secondary structure Click Save and Submit to save and submit. Click Save All Ansuers to save all anscers 7977 Mostly cloodyWhich way is more common practice to characterize the strength of a binding reaction between a protein and its ligand? Group of answer choices By its binding free energy, delta G By its equilibrium association constant K(A) By its equilibrium dissociation constant K(D) By the rate at which the biding reaction proceedsWhich of the following is/are advantages of multienzyme complexes? Which of the following is/are advantages of multienzyme complexes? None of the options are advantageous They speed up reaction rates. Side reactions are limited by channeling The entire complex can be controlled as one unit.
- Which of the following is the most probable catalytic triad of an enzyme that follows general acid base catalysis? -Glu-His-Cys -Leu-His-Ser -Glu-Phe-Ser -Asp-His-Ala -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -Which of the following cofactors will eventually dissociate from their enzyme polypeptide given enough time in a dilute solution? TPP NAD+ FAD Coenzyme A Biotin Lipoic AcidGiven the active site diagram below, which best described the mechanism(s) of Active Site `NH2. SH OH - catalysis? NH -Mg²+ O Acid-Base O Acid-Base & Metal lon Covalent Catalysis Acid-Base & Covalent Catalysis O Metal lon
- True or False Immobilization improves the stability of the enzyme. EnaLne, has a half-life of 10 days in free solution, but under identical conditions of temperature, pH, and medium composition, the measured half-life of a packed column is 30 days. The enzyme is immobilized in a porous sphere 5 mm in diameter.A Leu side chain can form Schiff base with the substrate during covalent catalysis. True FalseProtease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn Erase