Please discuss the following statement. "If two ligands involve in the same number and type of attractive interactions within the binding site, then both will have similar potency" State if this statement is true or false, then explain your answer
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- Pls help ASAP, thank you! "Regulation of metabolic pathways most typically occurs at enzyme steps that are"Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, IIIDraw a schematic diagram illustrate the interactions made between the key components of total and non- specific binding reactions. Should reflect on the role of each of the components of the reaction mixures and why the substration of non-specific binding from total binding allows us to calculate specific binding.
- How does ground state destabilization, transition state stabilization, and proximity lead to catalysis???? Also, I know binding affinity helps to bind targets selectively and specifically but what's their job in catalysis?Enzyme specificity (list the different types of enzyme specificities)Let’s consider vmax. Recall that uncompetitive inhibitors bind to the enzyme only after thesubstate is bound.a) As the concentration of substrate increases, the fraction of enzyme bound to substrate (circleone) increases / decreases?b) Does an uncompetitive inhibitor bind more readily when the substrate concentration is low orhigh?
- Explain and differentiate the lock-and-key and induced fit models for binding of a substrate to an enzyme. If only a few of the amino acid residues of an enzyme are involved in its catalytic activity, then why does the enzyme need such a large number of amino acids?Identification of the active site of an enzyme - which methods do scientists use today to identify the active site?Question: What type of enzyme inhibitor is Quinapril ?
- What is the fractional occupancy of a protein binding site when the ligand concentration (L) =1mM and the ligand equilibrium binding constant at the binding site K10= 10microM. 0.01 B.0.1 C.0.91 D.0.99 none of the listed valuesunderstanding Biomolecules for development of biosensors and their application, how this will advance our knowledge of the subject?23. Which is not a function of proteins: a) catalyzing reactions b) structural properties such as mechanical strength, shape, flexibility c) carries genetic information d) movement or contraction