Lecture 8/01.31.25 Flashcards
(19 cards)
What is true about protein folding?
It is favorable, thus negative
What happens when proteins are denatured?
They attempt to go back to its native form
How does protein folding occur?
It is a fast process that is not random and is sometimes mediated.
What is chaperonin?
It helps proteins fold correctly during stressful conditions
What are hsp?
Heat shock proteins that help prevent denaturing
How does chaperonin work?
GroEL binds to unfolded proteins via hydrophobic residues. Then, ATP and GroES causes conformation to hide hydrophobic residues and forces protein into hydrophilic chamber causing residues to hide and induce folding.
What happens when proteins don’t fold properly?
They form amyloids and later diseases like alzheimer’s or parkinson’s
What is quaternary structure?
It is where proteins are made up of more than one subunit that is held together by patches of noncovalent bonds
What is called when two subunits are the same?
homodimer
What is it called when two subunits are different?
heterodimer
Where do we get proteins from?
Extracting from cells and later purify them
How do we extract from cells?
We can break them from high frequency sound, mild detergent, force, or mortar/pestile to grind up the cell wall or bilayer. This is also called homogenization
What happens after extracting the protein?
Put into a centrifuge and spun and removed supernatant each time
What is zonal centrifugation?
It is centrifugation that separates matter according to density
What do we do after centrigugating?
Salting out the protein but not too much because it will make it into a precipitate
What do we after salting out the protein?
Purification by chromatography
What happens after purification?
The chromatography will separate it by size and/or shape differences
What is ion-exchange chromatography?
It separated mainly by charge difference between proteins.
What is affinity chromatography?
It is where natural non-covalent interactions is used to purify proteins
