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The thermodynamic box (linked functions diagram) below shows all the possible dissociation equilibria for an enzyme-bound reversible inhibitor and substrate (the ESI complex). Kİ' B.KI, and KES' =B KES Keat K1 E+S kı k-1 KES ES + K'₁ = BK₁ P+E I For the ß ranges/values below, fill in the type of inhibition (competitive, uncompetitive, mixed, or special case of mixed: "pure noncompetitive". Describe briefly in qualitative terms (not equations) how changing ß changes the relative binding affinities of I and S to different species (E, ES, and EI), and explain in terms of relative values of KI and KI

The thermodynamic box (linked functions diagram) below shows all the possible dissociation equilibria for an enzyme-bound reversible inhibitor and substrate (the ESI complex). Kİ' B.KI, and KES' =B KES Keat K1 E+S kı k-1 KES ES + K'₁ = BK₁ P+E I For the ß ranges/values below, fill in the type of inhibition (competitive, uncompetitive, mixed, or special case of mixed: "pure noncompetitive". Describe briefly in qualitative terms (not equations) how changing ß changes the relative binding affinities of I and S to different species (E, ES, and EI), and explain in terms of relative values of KI and KI

Chemistry
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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Can you please help find the type of inhibition for these two question?
The thermodynamic box (linked functions diagram) below shows all the possible dissociation equilibria for an enzyme-bound reversible inhibitor and substrate (the ESI complex). Kİ' = B•KI , and KES' =B•KES %3D kı kent For the B ranges/values below, fill in the type of inhibition (competitive, uncompetitive, mixed, or special case of mixed: "pure noncompetitive". Describe briefly in qualitative terms (not equations) how changing B changes the relative binding affinities of I and S to different species (E, ES, and EI), and explain in terms of relative values of KI' and KI, and of KES' and KES. E+S ES P+E KES KI K'I = BK1 El + S ESI --X-- P+ EI K'ES = BKES
Transcribed Image Text:The thermodynamic box (linked functions diagram) below shows all the possible dissociation equilibria for an enzyme-bound reversible inhibitor and substrate (the ESI complex). Kİ' = B•KI , and KES' =B•KES %3D kı kent For the B ranges/values below, fill in the type of inhibition (competitive, uncompetitive, mixed, or special case of mixed: "pure noncompetitive". Describe briefly in qualitative terms (not equations) how changing B changes the relative binding affinities of I and S to different species (E, ES, and EI), and explain in terms of relative values of KI' and KI, and of KES' and KES. E+S ES P+E KES KI K'I = BK1 El + S ESI --X-- P+ EI K'ES = BKES
C. B=1 Type of inhibition: D. 1<B< infinity Type of inhibition:
Transcribed Image Text:C. B=1 Type of inhibition: D. 1<B< infinity Type of inhibition:
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