Rank these substrates in order of best inhibitor (highest binding affinity) to worst inhibitor (lowest binding affinity).Rank from highest binding affinity to lowest binding affinity. To rank items as equivalent, overlap them. You have determined the \( K_I \) value for NSMAB for PaESBL-1. You now repeat this inhibition experiment with several additional boronic acid analogs. The experimentally determined \( K_I \) values for these additional inhibitors are provided in the table:| Boronate analog | \( K_I \) (nM) ||-----------------|----------------|| Inhibitor A | 7.3 || Inhibitor B | 110 || Inhibitor C | 0.32 || Inhibitor D | 25 || Inhibitor E | 570 || Inhibitor F | 3200 |The table lists the boronate analogs as inhibitors and their corresponding \( K_I \) values in nanomolar (nM). Lower \( K_I \) values indicate stronger affinity between the inhibitor and the enzyme, suggesting higher inhibitory potency. The image displays a sequence of labeled buttons, which could represent a list of chemical inhibitors and a compound:- Inhibitor C- Inhibitor A- Inhibitor D- NSAMB- Inhibitor B- Inhibitor E- Inhibitor FThese labels might refer to various inhibitors used in biological or chemical processes. NSAMB could stand for a specific compound or category differing from the inhibitors. Further context would be needed to understand their specific roles or applications.

Ki is the inhibitor constant, that tells how potent an inhibitor is. It gives an idea of the…

Rank these substrates in order of best inhibitor (highest binding affinity) to worst inhibitor (lowest binding affinity). Rank from highest binding affinity to lowest binding affinity. To rank items as equivalent, overlap them.

Rank these substrates in order of best inhibitor (highest binding affinity) to worst inhibitor (lowest binding affinity). Rank from highest binding affinity to lowest binding affinity. To rank items as equivalent, overlap them.

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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I have a fill in the blank question. "1) Heterophobic or Homotrophic effects= are changes in affinity due to substrate binding and cooperativity between different subunits. They give Allosteric rate curves their Sigmoid shape. 2) Hetero or Homotrophic effects=are changes in affinity due to binding of an effector to an Allosteric site. Allosteric sites are usually 3)located outside or inside the active site. Positive Allosteric effectors (activators) shift the rate curve 4) Left or Right, where Negative effectors shift it 5) right or left. Positive Allosteric effectors usually stabalize the 6)T or R state. Negative efftors usually satbalize the R state." Thank You!!!
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