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II. While there are many different types of inhibitors, most have a very similar structure so they can compete with the normal substrate (in this case dopamine). Of the molecules below, which compound do you think has the most promise as an inhibitor? HO a.a.#1 N- H a.a.#2 H₂PO3 -PO₂H₂ OH Alendronate a.a.#6 NH₂ Carbidopa Using the same, amino acid orientation as you arrived at for Part I, show which inhibitor is most promising a.a.#5 Raloxifene a.a.#3 a.a.#4

II. While there are many different types of inhibitors, most have a very similar structure so they can compete with the normal substrate (in this case dopamine). Of the molecules below, which compound do you think has the most promise as an inhibitor? HO a.a.#1 N- H a.a.#2 H₂PO3 -PO₂H₂ OH Alendronate a.a.#6 NH₂ Carbidopa Using the same, amino acid orientation as you arrived at for Part I, show which inhibitor is most promising a.a.#5 Raloxifene a.a.#3 a.a.#4

Biochemistry
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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II. While there are many different types of inhibitors, most have a very similar structure so they can compete with the normal substrate (in this case dopamine). Of the molecules below, which compound do you think has the most promise as an inhibitor? HO a.a.#1 C a.a.#2 N- H H₂PO OH Alendronate a.a.#6 NH₂ -PO₂H₂ Carbidopa Using the same, amino acid orientation as you arrived at for Part I, show which inhibitor is most promising Car a.a.#5 a.a.#3 Raloxifene a.a.#4
Transcribed Image Text:II. While there are many different types of inhibitors, most have a very similar structure so they can compete with the normal substrate (in this case dopamine). Of the molecules below, which compound do you think has the most promise as an inhibitor? HO a.a.#1 C a.a.#2 N- H H₂PO OH Alendronate a.a.#6 NH₂ -PO₂H₂ Carbidopa Using the same, amino acid orientation as you arrived at for Part I, show which inhibitor is most promising Car a.a.#5 a.a.#3 Raloxifene a.a.#4
I. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4
Transcribed Image Text:I. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4
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