Term
| What is the native state of a protein? |
|
Definition
| the fully folded, least energy form of a protein |
|
|
Term
| What is the denatured form of a protein? |
|
Definition
| The unfolded form of a protein |
|
|
Term
Protein Denaturing:
How can a protein be denatured? |
|
Definition
-High temperature
-Chemical (guanidinium, urea, detergents [SDS], organic solvents)
-pH |
|
|
Term
Subunit Interactions:
What is protein aggregation? How is it avoided? |
|
Definition
-When subunits un-wantedly come together
-Adding like-charges to the subunits so they repel one another |
|
|
Term
Subunit Interactions:
Which intermolecular forces influence quaternary structure? |
|
Definition
| -Hydrophobic effect -Hydrogen bonding -Electrostatics (salt bridges) -Van Der Waals forces (dipoles) |
|
|
Term
Subunit Interactions:
What AA's do H-bonding in quaternary structure? |
|
Definition
| -Polar, neutral AA's (N, Q, Y, T, S) |
|
|
Term
Subunit Interactions:
What AA's do salt bridging in quaternary structure? |
|
Definition
| -Acidic (D, E) and basic (K, R, H) AA's |
|
|
Term
|
Definition
| Unfolds proteins by disrupting the polar interactions in the protein (not covalent bonds) |
|
|
Term
|
Definition
| Highly polar, increasing solubility of hydrophobic areas and competing with intermolecular H-bonding by bonding strongly to amides |
|
|
