Alain 2 Flashcards
Wt’s inverse agonist?
A molecule binding to the same side of agonist. However, it elicits opposite effect.
Primary structure of Protein?
Peptide bond between amino acids.
There are Aliphatics, hydrophilic, aromatic anf other a.a.
How many common a.a. found in human?
20
Trans or cis conformation are favoured?
C-N bond in peptide group could not rotate freely due to resonance effect. Trans conformations are favoured because its steric interaction is small.
If there is H-bond, sometimes cis is favoured.
How 3D struc of Pro. is Impo.?
It is crucial to Pro. func. and interaction with drug.
Why 2 Cys could be closed tog. to form disulfide bond?
They are not close tog. but due to Po. folding they become close tog and then form the bond via oxidation.
Why the relative effect of bonding force are opposite to what we are expected?
They interact with water.
polar groups are not free!
Which is more imp. to pro. function, struc. or sequence?
Pro. Struc.
Wt could occur during translation at ribosom?
Translational pro. modification (Cofactor binding, hydro., acetyl., oxid., glyc., phos., sulf., iod., ADP ribosylation, carbo.)
Most imp. drug TG are
enzymes and receptors
Func. of Pro.
- Enzyme
- Receptor
- Structural Pro.
- Transport Pro.
- Ion channels.
- Others
Accelarating factor =
k (cat)/ k (non cat)
2 role of a.a. at active site:
- Binding (binding the substrate to the active site)
2. Catalytic (involve in the mechanism of react.)
How do Enz. lower activation Ene?
- Provide suitable enviro.
- Bring reactants together.
- Position reactants correctly.
- Weaken bond.
- Participate in mechanism.
Enz. Cat. ability is provided by
- Residues
- Cofactor (to activate apoenzyme)
+ Metal
+ Coenzyme (usually vitamin) - org. molecule
