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2.2  Architecture of Organisms, Tissues, and Cells and the Bits Between

So, there is some interesting size regulation occurring, which links droplet biophysics and

their biological functions. LLPS droplets in effect are a very energy efficient and a rapid way

to generate spatial compartmentalization in the cell since they do not require a bounding lipid

membrane, which is often slow to form and requires energy input. Instead, LLPS droplets

can form rapidly and reversibly in response to environmental triggers in the cell and can

package several biomolecules into one droplet to act as a very efficient nano-​reactor bio­

chemical vessel since the concentration of the reactants in such a small volume can be very

high. LLPS droplets research is very active currently, with droplets now being found in many

biological systems and being associated with both normal and disease processes. As you will

see from Chapter 4, research is being done using super-​resolution microscopy to investi­

gate these droplets experimentally, but as you will also see from Chapter 8 much modeling

computational simulation research tools are being developed to understand this interesting

phenomenon.

2.2.7  VIRUSES

Worked Case Example 2.1: Biomolecular Liquid Condensates

One type of biomolecule B dissolved in solvent S has an exothermic interaction enthalpy

of 3kBT between 2 B molecules, 2kBT between 2 S molecules, and 1.5 kBT between 1 B and

1 S molecule. If there are no differences between the number of accessible microstates

between well-​mixed and demixed, what is the probability that a well-​mixed solution of B

will phase separate? Assume each B or S molecule must either bind to another B molecule

or an S molecule.

Answer:

With no difference in the number of accessible microstates between well-​mixed

and demixed, this implies that here there is no entropy difference upon phase tran­

sition, and so the likelihood of phase transition occurring is determined solely by

the net enthalpic differences. To determine the probability of a transition for any

thermodynamic process, we use the Boltzmann factor since the probability of any

transition occurring, which has a total free energy activity barrier of E, is propor­

tional to the Boltzmann factor of exp(–​E/​kBT) where kB is the Boltzmann constant

and T the absolute temperature. So, the total probability for phase separation

occurring is given by the sum of all relevant Boltzmann factors for phase separ­

ation to occur, divided by the total sum of all possible Boltzmann factors (i.e. for all

transitions for demixing of the biomolecules and the solvent molecules in phase

separation, but also for those for well-​mixed solvent with biomolecule)—​for those

acquainted with statistical physics, this sum is often referred to as the parameter

Z, known as the canonical partition function (often omitting the word “canonical”)

and here in effect serves as a normalization constant to generate the probability.

We are told that each B or S molecule must either bind to another B or S molecule.

Thus, the possible combinations of molecule pairs are SS, BB, SB or BS. SS and BB are

demixed, SB and BS are well-​mixed. Interaction enthalpies here are all exothermic

(attractive), so the associated energy barriers are all negative: –​2.0, –​1.5. –​1.5. –​3.0

kBT. The phase transition probability therefore goes as:

exp

E

k T

exp E

k T

exp

E

k T

exp

E

k T

exp

SS

B

BB

B

SS

B

BB

B

(

)

(

)

(

)

(

)

(

+

+

+

/

/

/

/

+

E

k T

expt E

k T

SB

B

BS

B

/

/

)

(

)

After substituting in the values given, this probability comes out as ~0.75, or 75%.

This sort of analysis doesn’t of course give you any information about the spatial

dependence of droplet formation. But it does illustrate that relatively small energy