Atetrameric protein dissociates into dimers when the detergent sodium dodecyl sulfate (sds) is added to a solution of the protein. but the dimers are termed sds-resistant because they do not further dissociate into monomers in the presence of the detergent. what intermolecular forces might be acting at the dimer-dimer interface? are the intermolecular forces acting at the monomer-monomer interface different? explain.

At the dimer-dimer interface there might be acting non-covalent forces (van der waals, Hidrogene bridges, hydrophobic forces)

At the monomer-monomer interface there might be covalent forces acting (disulfide bridges).

Explanation:

On the SDS-PAGE application  works by disrupting non-covalent bonds in the proteins, and so denaturing them. Therefore, the disulfide bridges won´t be disrupted, so the monomers will remain bounded.

electrical potential energy =0.072 j

explanation:

electrical potential energy is given by

u= q δv

q= charge=6 c

δv= potential difference and is given by

δv= e d

e= electric field

d= distance=5 mm=0.005 m

δv=2.4 (0.005)=0.012 v

now electric potential energy= u= q δv

u=6 (0.012)

u=0.072 j