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Assignments Biophysics 2
Assignments Biophysics 2
Assignments Biophysics 2
1. Show that if a charged liquid drop evaporates into the air, there will come a point at
which it will become unstable and break up into smaller charged droplets. This is known
as the Rayleigh limit. If the charge on the drop is Q = 100e and the liquid is water that
has a surface tension of γ = 73 mN m−1 (Numerically equal to the surface energy in
units of mJ m−2 ), at what drop radius R will this happen and what will be the nature of
fragmentation? [Hint: Chapter 3 of Intermolecular and Surface ForcesIntermolecular
and Surface Forces by J. N. Israelachvili ]
3. Two nonpolar solute molecules 1 and 2 interact in a slightly polar medium 3 at 298 K.
The interaction is dominated entirely by van der Waals forces, and the molecules may
be considered to behave as small spheres with the same dielectric properties as the bulk
materials whose properties are n1 = 1.40, n2 = 1.50, n3 = 1.45, ε1 = n21 , ε2 = n22 ,
and ε3 = 6.0. If the absorption frequency νe of all three media is the same and equal to
3×1015 s−1 , will the equilibrium interaction potential be (a) attractive at all separations,
including contact, (b) repulsive at all separations, including contact, or (c) repulsive at
small separations but attractive (adhesive) at some finite separations?
If your answer is (a) or (c), is the adhesion energy strong enough to lead to aggregation
or phase separations of the solute in the solvent above some critical concentration (the
solubility)? [Hint: Chapter 6 of Intermolecular and Surface Forces Intermolecular and
Surface Forces by J. N. Israelachvili ]
4. Polymethylene oxide, [−CH2 − O−]n , is hydrophobic, but polyethylene oxide, PEO
[−CH2 − CH2 − O−]n , which has one more hydrophobic CH2 group per segment, is
hydrophilic and miscible with water. Give a possible reason for this. [Hint: Chapter
8 of Intermolecular and Surface ForcesIntermolecular and Surface Forces by J. N. Is-
raelachvili ]
5. A globular, water-soluble protein has surface residues consisting mainly of Asp, Glu,
His, and Ser. (i) Would you expect the folding rate of the protein to increase or decrease
at a higher pH? (ii) If the protein is also involved in a specific (receptor-ligand type)
binding interaction involving a hydrophobic pocket on the protein, how would you expect
the on-rate kon , off-rate kof f , and overall reaction constant K to be affected (increased
or decreased) at the higher pH? [Hint: Chapter 22 of Intermolecular and Surface
ForcesIntermolecular and Surface Forces by J. N. Israelachvili ]
Best wishes
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