How does protein flexibility relate to function?
Protein movement often involves:
2. Making/breaking of non-covalent interactions as the protein moves or subunits move relative to one another
Triggered conformational changes are dependent on :
2. Inherent flexibility/ instability of molecules
Molecular recognition depends on:
Structure of binding sites
For marcomolecules shape of binding site can be:
Concave, convex or flat and may be grooves
For small molecules shape of binding site can be:
Clefts, pockets or cavities
Catalytic active sites
Occur at the interface between subunits or domains in proteins.
Weak interaction between ligand and protein
Favors easy exchange of molecules
The energy for driving binding events is provided by
Displacement of water from ligand binding site
Kd =
The equilibrium constant for the release of ligand
[P.L]/[Po]
Proportion of protein that has ligand-bound
Relationship between [P.L]/[Po] and [L]
Rectangular hyperbola
Equation for ligand binding
[P.L]/[Po] = [L]/ [L] + [Kd]
Units of Kd
Molar concentration e.g. Moles/litre
The lower the value of Kd
The higher the affinity of the ligand for the protein