hanges in delta-S for the folding of a protein is positive and provides the most significant contribution to thermodynamic driving force for folding. True or False
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A: Reaction: 2H₂O₂(aq) → 2H2O(l) + O2(g)Km = 25 mMTurnover number Kcat = 4.0 × 107s–1Total enzyme…
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A: Given values: K1 = 8×108 M-1sec-1 K-1 = 2×105 sec-1 K2 = 1×102 sec-1
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Q: what is the Vmax and Km of the enzyme in the reaction
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Changes in delta-S for the folding of a protein is positive and provides the most significant contribution to
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- Regarding the physical condition (characteristics of the solution/environment) in which an enzyme finds itself: sometimes enzymes are most active at a certain level and still active but to a lesser degree at a level above or below the optimal level. Describe the likely reason for the enzyme’s decrement in function at levels other than the optimal level?this is not a writing assignment or essay just give a brief explanationNumber 4 please
- Discuss the advantages and disadvantages of Protein efficiency ratio(PER)Denatured protein is in a low energy state. What sort of explanation can you use to rationalize that statement? Hint: consider Gibbs free energy.affinity of a protein-protein or protein-ligand interaction can be described by the Dissociation Constant, Kd (written below). Consider a protein P and its inhibitor, I. I inhibits P's activity when bound to it: koff _ [A][B] Dissociation Constant: Ka = koN [AB] Question When [I] is 10-7 M, 99% of P's activity is inhibited. What is the Kd of this Protein- Inhibitor interaction?
- "Enzymes that undergo cooperative allosteric transitions invariably consist of symmetric assemblies of multiple subunits" is true or false.Which 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 proceedsDescribe with detail the chemical reactions of 5 proteins that are involved in human metabolic disorders. Explain in detail the interaction mechanisms with their corresponding substrates, their reaction mechanisms, and chemical regulations.
- "Binding of extracellular ligands to receptor tyrosine kinases (RTKs) activates the intracellular catalytic domain by propagating a conformational change across the lipid bilayer through a single transmembrane a helix" is true or false.Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.Color Reactions of Intact Protein: 1ml of water and 0.5 g of casein 1ml of water and 0.5 g of bean protein 1ml of water and 0.5 g of gluten