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21 Cards in this Set

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  • Back

What is the definition of an agonist?

Chemicals that interact with a biomolecule in a way that entices/induces that biomolecule to perform its normal function

What is the definition of an antagonist?

Chemicals that interact with a biomolecule in a way that prevents that biomolecule from performing its normal function. By definition, most inhibitors are antagonists.

What is an enzyme?

A biomolecule, usually a protein (polypeptide), that lowers the activation energy of a reaction, and therefore is a catalyst.

Is an enzyme consumed in a reaction?

No.

What is a receptor?

Biomolecules that "change" when bonded to another molecule.

What are the 4 main classes of drug targets?

Enzymes, receptors, other proteins, nucleic acids.

What other protein targets are there other than enzymes and receptors?

Transport proteins, chaperones, protein-protein interactions.

How would we target nucleic acids?

A DNA damaging agent. It would usually be lethal to cells, which is great for chemotherapy.

What is the definition of a drug?

Chemicals that are recognized (if not approved) by a legitimate regulating agency as having a medical effect.

What is the definition of Drug candidates/Development candidates?

Chemicals that are under investigation as potential drugs.

What is the definition of a Xenobiotic?

Chemicals that are not natural, or are present in abnormally high concentrations, in an organism.

What is the definition of a ligand?

Chemicals that bind with a biomolecule.

What is the definition of a substrate?

Chemicals that bind to and are changed by a biomolecule.

What is the definition of products?

Chemicals that are formed as the result of a reaction.

What are the two main secondary structures of enzymes formed?

They typically take on two types of secondary structures based on hydrogen bonding, α-helices and β-sheets

They typically have a __________ shell that protects a _________ pocket, where most of the enzymatic activity occurs.

They typically have a “hydrophilic” shell that protects a hydrophobic pocket, where most of the enzymatic activity occurs.

What is the name of the hydrophobic pocket of the enzyme where the enzymatic activity occurs?

The Active Site.

What are the bond strengths of Covalent, Ionic and hydrogen bonds?

Covalent bonds - > 200 kJ/mol


Ionic bonds - ~ 30 kJ/mol


Hydrogen bonds - ~ 20 kJ/mol

What are the strengths of the interactions of Dipolar and London/Van der Waals interactions?

Dipolar interactions - ~ 5 kJ/mol


London/Van der Waals interactions - ~ 3 kJ/mol

Enzymes: What does a competitive inhibitor do?

It interferes with the active site of the enzyme so substrate cannot bind.

Enzymes: What does a non-competitive inhibitor do?

It changes the shape of the active site so it can't bind to the substrate.