Now let's look at the specific amino acid interactions at the dimer interface that link the two monomers together into the larger homodimer structure. Which of the following accurately describes the specific interactions that stabilize the dimer structure?

a) Ionic bonds between phe106 and ile108 of one monomer and ile272 and leu273 of the other monomer. Hydrophobic interactions between arg96 and arg103 of one monomer and glu300 and glu304 of the other monomer.
b) Hydrophobic interactions between phe106 and ile108 of one monomer and ile272 and leu273 of the other monomer. Ionic bonds between arg96 and arg103 of one monomer and glu300 and glu304 of the other monomer.
c) Hydrophobic interactions between phe106 and ile108 of one monomer and ile272 and leu273 of the other monomer. Hydrophobic interactions between arg96 and arg103 of one monomer and glu300 and glu304 of the other monomer.
d) Ionic bonds between phe106 and ile108 of one monomer and ile272 and leu273 of the other monomer. Ionic bonds between arg96 and arg103 of one monomer and glu300 and glu304 of the other monomer.

Correct answer is B

Explanation:

 A dimer is a molecule consisting of two identical halves, formed by joining two identical molecules, sometimes with a single atom acting as a bridge.

A monomer is a relatively small molecule which can be covalently bonded to other monomers to form a polymer.

Specific amino acid molecular interactions at the dimer interface differs from species to species and from phase to phase here are some possibilities of the hydrophobic effect;

• no net change in favorable or unfavorable molecular interactions leading to decrease in rotational, translational, vibrational degrees of freedom of water (or some free radicals)

• increase in favorable molecular interactions of bridge (maybe cyclohexane) causing a decrease in rotational, translational, vibrational degrees of freedom of bridge (cyclohexane)

Entropy change is key to molecular interactions of these kinds. The molecular interactions of dimer-interface of amino acid residues are important for the stability of the enzyme function it contribute to the subunit-subunit interactions in this or the conformational stability of the monomersin context.

According to the question,

Hydrophobic interactions between phe106 and ile108 of one monomer and ile272 and leu273 of the other monomer explains the hydrophobic effect.

Ionic bonds between arg96 and arg103 of one monomer and glu300 and glu304 of the other monomer explains the steric effect for stability.

The bridge between these above gives a solid dimer polymer.

the match duh

explanation: