Non-Covalent Interactions in Proteins

These flashcards cover essential vocabulary related to non-covalent interactions in proteins, including definitions and descriptions of key concepts.

Native State

The most stable folded conformation of a protein.

Intrinsically Disordered Proteins

Proteins that do not have stable structures.

Salt Bridges

Electrostatic interactions between ionized carboxyl groups and guanidinium ions.

Hydrogen Bonds

Attractive forces formed when two electronegative atoms compete for a hydrogen atom.

Van der Waals Interactions

Attractive forces due to transient dipoles in atoms.

Hydrophobic Effect

The tendency of non-polar molecules to aggregate in aqueous solutions to minimize disruption in the water structure.

Electronegativity

A measure of the tendency of an atom to attract a bonding pair of electrons.

Dielectric Constant

A measure of a substance's ability to insulate charges from each other.

pKa

The pH at which half of the species are deprotonated.

Protein Unfolding

The process by which proteins lose their 3D structure due to extreme pH or temperature changes.