Basic Physical Scales Relevant to Cells and

Molecules
Relevant Length Scales
The basic length scale used to describe molecules is a nanometer (1 nanometer = 1 nm = 10-
9 meters)

Many biomolecules are made out of chemical units (e.g. nucleotides, amino acids) which are
around 1 nm in size, meaning that they are a few atoms across. Other `small' molecules such as
lipids and sugars are also roughly on this length scale. Most folded up proteins are a few nm in
diameter. So, the nanometer is really useful as a basic yardstick of biomolecules.
Another commonly used unit of length is the Angstrom (1 Angstrom = 10-10 m = 0.1
nanometer). Atoms are roughly Angstroms in size (a hydrogen atom is about 1 A in diameter, a
carbon atom is about 2 A in diameter).

Thermal Energy
Each microscopic degree of freedom has an energy kBT associated with it

At room temperature, molecules are jiggling around continually due to thermal motion. In cells,
everything is surrounded by water and so everything is being bumped continuously by
neighboring molecules. All of this random motion gives rise to diffusion of individual
molecules..

The energy associated with a single molecular degree of freedom, e.g. the linear motion of a
molecule, or the energy of stretching of a chemical bond, is a fundamental physical quantity:

kBT = (Boltzmann's constant) x (absolute temperature)

Here Boltzmann's constant is kB = 1.38 x 10-23 Joules/Kelvin, and is a fundamental constant

determined experimentally.

Remember that room temperature (25 C) in absolute terms is around 300 Kelvin (25 + 273.1 =
298.1 K to be more precise).

So kBT = 4.1 x 10-21 J is the relevant thermal energy of single molecular degrees of freedom

We can roughly estimate the velocity with which a water molecule is moving in a glass of water
(or in a cell) at 300 K.
Between collisions, a water molecule has kinetic energy which will be about the thermal energy:
 m v2
= kB T
2

which means that the velocity will be about

2 kB T 1/2 2 4 1021 J 1/2
v= = = 530 m/sec
m 18 1.6 1027 kg

Relevant Time Scales

The time between collisions of small molecules in a liquid is about a picosecond

The typical time between successive collisions of a water molecule with its neighbors. We
simply have

x
=v
t

where x = 0.2 nm is the rough size of a water molecule, and where v = 500 m/sec.
Rearranging and solving for the time interval gives t = 0.4 x 10-12 sec, about half a picosecond.

Over times longer than one collision time, molecules undergo random-walk or diffusive
motion

After one collision, the direction of our water molecule will be changed in an difficult-to-predict
way. After a few collisions there will be no chance to predict its direction of motion, or even
where it is. This process is called diffusion, and we will discuss it in detail later. Diffusive
motion is totally different from the straight-line motion we just considered. We'll see that a
diffusing molecule has a relation between distance covered x and time interval t which is

(x)2
=D
t

where D is the diffusion constant, with units length-squared per time, for that molecule. For a
water molecule in water we can estimate its diffusion constant very roughly as
(0.2 nm)2
D= = 1 x 10-3 (cm)2/sec
-12
0.4 x 10 sec
A key point about diffusion is that the time you have to wait to go a distance x grows as the
square of that distance. So diffusion is increasingly slow at longer and longer distances.

Similarly, motion of larger molecules (e.g. large proteins or nucleic acids) occurs essentially by
diffusion, in the absence of other forces. Biomolecules which are flexible additionally undergo
random shape changes. We'll see that even moderately long molecules - a few thousand repeat
units - can take microseconds to milliseconds to move.

Relevant time scales for us will include the time that it takes chemical reaction to occur, which if
there are large energy barriers to cross, can be seconds or longer.

Stored Energy in Cells

Cells don't rely on thermal energy or thermal motion to move molecules around. Instead, they
harvest energy from their surroundings, and then store it until it is needed. One of the molecules
used to store energy for the short term is ATP, which can be converted to ADP in an exothermic
reaction which liberates about 20 kBT under cellular conditions. Very roughly ATP -> ADP
conversion steps are used to liberate energy to drive other chemical reactions in the cell.

So - cells use units of energy which are appreciably larger than single thermal excitations. This
is crucial to avoid having thermal motion simply bring the contents of a cell to thermal
equilibrium - meaning death.

Forces in Cells
A force is developed when work (with a change in energy) is done over a distance:
E
f=
x

We can use this to estimate the forces experienced by molecules during thermal fluctuations, and
during biological processes.

Generally we will be worried about energies on the order of a kBT, and distance over which such
energies are transferred of a nm. So we can see that the rough forces that we will be talking
about will be

f = 4x 10-21 J = 4 x 10-12 N = 4 piconewtons = 4 pN

 10-9 m

For random thermal motions, we already saw that the energy of a water molecule can change by
a fraction of kBT over a distance comparable to its size of 0.1 nm, so water molecules are subject
to random forces that instantaneously may be a few tens of pN.

For directed motions generated by e.g. burning of ATP in the cell, the steps will be a nm or so,
and the energy used per step will be a few kBT, again giving forces in the few pN range.

Hydrodynamic Drag, Brownian Motion and

Diffusion
Drag, diffusion, and Brownian motion are intimately related. Since they all bear on the motion of
small objects in an aqueous environment, they are of paramount importance to understanding
cellular processes. The basic formulae presented below are applicable from the micron scale
down to the nanometer scale and below.

Fluid Viscosity

All fluids have a viscosity, which describes the amount of friction between nearby regions of the
fluid moving at different velocities. Viscosity is what causes dissipation of energy in
hydrodynamic flow: after you stir your coffee, it eventually stops moving, thanks to frictional
losses.

The units of viscosity are pressuretime, or mass/ (lengthtime). The cgs unit of viscosity is 1
g/(cmsec) = 1 Poise; the SI unit of viscosity is 1 Pasec.

It is useful to remember that 1 Poise = 0.1 Pasec (check this!)

Water, and solutions which are mostly water, have a viscosity close to water = 0.01 Poise or
0.001 Pasec. This value of viscosity will be used extensively, since the stuff around
biomolecules in vivo is mostly water. By the way, we should remember that water has a mass
density of water = 1 g/cm3 = 103 kg/m3.

Some fluid mechanics people and books talk about `kinematic viscosity' = /. We will never
use kinematic viscosity.

Reynolds Number

Consider hydrodynamic flow characterized by a fluid of some mass density, flowing at some
velocity, past an object of some length. The Reynolds number of the flow past the object (or
`wake') is the dimensionless combination
 velocitylengthmass density
Re =
viscosity

Alternately, the length used to estimate Re might be the width of a channel (or pipe) that fluid is
flowing through.

If Re >> 1 then the flow is turbulent, with complicated vortices and eddies at a wide range of
sizes which continually are reorganizing. Turbulence is not well understood at all, and will not
be discussed further, except for a simple example:

Example: What is Re in the wake of a sailboat? The fluid velocity is about 10 m/sec, the rough
length scale is 1 m, the density is 103 kg/m3 and the viscosity is 103 Pasec, thus Re 107.

Fortunately turbulence is largely irrelevant at molecular and cellular scales. The velocities and
lengths we will worry about end up just being too small to ever allow Re to get big.

Example: What is Re in the wake of a micron-sized particle moving at a velocity of 1

micron/sec?

106 106 103

Re = = 106
3
10

For sufficiently tiny things moving sufficiently slowly, Re << 1. In general, the situations
discussed in this course will be in this limit. This is great because for Re << 1, the equations of
hydrodynamics may be linearized and solved, and the solutions are meaningful.

Drag Coefficients for Re << 1

For Re << 1, the hydrodynamic drag force on a moving object is simply linearly proportional to
the object's velocity through the fluid, and being a frictional (or energy-dissipating) force, it acts
to oppose the motion. The drag force therefore looks just like the law of friction some of you
may remember from elementary physics courses:

fdrag d v

Here, is the viscosity, d is the longest dimension of the moving object, and v is the object's
velocity relative to the fluid. This formula neglects an overall numerical factor which depends on
the precise shape of the moving object; this factor is usually roughly 10.

The ratio of the drag force to the velocity (fdrag / v = kdrag) is called the drag coefficient, and is
roughly d.
Berg's book gives a nice tabulation of drag coefficients, but one particularly important case is
that of a sphere of radius R, for which the drag coefficient is kdrag = 6 R.

Example: Force needed to keep a bead moving at some velocity

Suppose a spherical bead of radius R moves at constant velocity v through a fluid of viscosity .
The force that must be supplied to keep the bead moving at that velocity must just balance the
drag force:

fdriving = fdrag 6 R v

For a 1-micron diameter bead moving at 10 microns/sec in water, this force must be (mks units)
fdriving = 6 3.14 103 106 105 = 19 1014 Newtons

or about 0.2 piconewtons (pN).

Brownian Motion

If you observe small (0.1 to 1 micron-radius) particles in water, you will see that they move
erratically - almost appearing to hop around discontinuously. This Brownian motion is due to
collisions with water molecules, which makes the particles undergo random-walk motion.

If we observe such a particle for a time interval t, we will see it displaced by a position vector r.
If we repeat this over and over again, we can compute the average displacement during time
interval t, and as long as no other forces (gravity, bulk hydrodynamic flow...) act, we should find
that

<r>=0

i.e. there is no preferred direction for the random forces exerted by the water molecules on our
particle.

The notation < > represents an average over many repeated and uncorrelated measurements.

So, we characterize Brownian motion not by the average displacement over some time, by
instead by the average displacement-squared:

< |r|2 > = 6 D t

where D is called the diffusion constant of the particle. This formula will be often referred to as
the `square-root law' of Brownian motion. The diffusion constant D depends both on the size and
shape of the particle, and on the viscosity and temperature of the fluid that it is moving through.
The factor of 6 is a convention, but an important one to remember. Also you should always
remember that diffusion constants have the dimensions of length2/time.

This law, and other quantitative features of Brownian motion, were established by a long series
of experimental works beginning with Robert Brown's original experiments of 1827. Much of
the crucial quantitative work was done by Jean Perrin in the early 1900s. Believe it or not,
interesting experiments on Brownian motion continue to be done today - you can read about
them in Nature, Science and other top research journals.

Here is a picture of the trajectory of a simulated Brownian particle projected into the x-y plane,
with D = 0.16 micron2/sec. The x and y axes are marked in microns. It starts from the origin
(x=0,y=0) at t=0, and the pictures show the trajectory after 1 sec, 3 sec and 10 sec:
Brownian trajectories are rough (actually `fractal'), and very unlike the smooth trajectories we
learn about in elementary mechanics courses. The roughness of the trajectories reflects the
underlying randomness of molecular motion. Here is the x-coordinate versus time for the
Brownian trajectory shown above:

This graph is x(t) for a random walk in one dimension, and could just as well represent how
much money you have in your pocket as you repeatedly play a game with equal odds.

The square-root-law is quite different from formulae of ordinary mechanics - you will probably
not measure a displacement-squared of exactly 6 D t in any one of your trials - this formula
represents only the average that you will obtain after many trials. However, it still makes sense
for us to say that a particle undergoing Brownian motion moves a distance (Dt)1/2 during a time
interval t.

The following figure shows the magnitude of displacement as a function of time for the
simulation of Brownian motion shown above (D = 0.16 micron2/sec). The rough curve is the
simulation; the smooth curve shows the average behavior, ( < |r|2 > )1/2 = (6 D t)1/2. Note that
although there are large fluctuations away from the average behavior, the Brownian motion tends
to grow, roughly following the smooth curve.

Problem: A particle has a diffusion constant of

D = 0.3 micron2/sec. How far can we expect it
to be displaced from its initial position after 1
second, 10 seconds, 100 seconds, 1 hour and 1
day?

Problem: Consider a particle which undergoes

Brownian motion in three dimensions with <
|r|2 > = 6 D t. Explain why < x2 > = < y2 > = < z2 > = 2 D t.

Problem: A particle undergoing Brownian motion is observed in a microscope, which of course

gives only xy information about position. From a series of measurements, < x2 + y2 > is
determined to grow linearly in time, with a slope of 3.2 108 cm2/sec. What is the diffusion
constant D for the particle?

Einstein's relation between drag coefficient and diffusion constant

In his Ph.D. work at the ETH in Zurich in 1905, and in two subsequent papers published in
Annalen der Physik in 1905 and 1906, Einstein established the theory of Brownian motion.
These two papers are more heavily cited than his papers on relativity, due to their wide
applicability (biology, chemistry, physics, chemical engineering...) and are the theoretical
foundation of chemical and colloid physics.

There were two immediate and big results of Einstein's thesis work. First, he provided a new way
to estimate Avogadro's number, which in 1905 was only known roughly. The idea that there
were molecules at all was still controversial in 1905.

Second, Einstein showed that the diffusion constant D of a small particle was simply related to
its drag coefficient kdrag and absolute temperature:

kB T
D=
kdrag

This impossibly simple formula is fundamental to the description of virtually all transport
phenomena - from biophysics to astrophysics! This formula is also sometimes called an `Einstein
relation', or a `fluctuation-dissipation formula'. Remarkably, this result was derived by William
Sutherland almost simultaneously in 1905.

It makes good sense that the rate at which a particle diffuses by Brownian motion will go up if its
drag coefficient is reduced, since the water molecules hitting it will bonk it further and faster.
Similarly, if absolute temperature is increased, then the amount of momentum transferred per
bonk will be larger, and D should therefore increase.

Example: What is the diffusion constant of a 1 micron-radius particle and a 1 nm-radius particle,
both in water at room temperature?
The Einstein relation tells us that the 1-micron particle has a diffusion constant of

kB T 4 1021
D= = = 0.2 1012 m2/sec
3 6
6 R 6 3.14 10 10
or equivalently D = 0.2 microns2/sec. This tells us that a 1-micron-radius particle in water is
displaced by 1 micron in about 5 seconds.

Since D is inversely proportional to R, the 1 nm-radius particle has a 1000-fold larger diffusion
constant, D = 200 microns2/sec. This means that in one second, our 1 nm-radius particle is
displaced about 15 microns.

Non-covalent interactions
We have learnt that all biological macromolecules are linear polymers in which repeating
subunits are covalently linked together. The free energy associated with a covalent bond is ~ 100
150 kBT. These bonds are therefore not disrupted by thermal fluctuations.

There are many, much weaker, non-covalent interactions that are responsible for the 3-
dimensional configuration that the biological polymers adopt. These interactions also play a very
important role in the flexibility of the macromolecules, their interactions with each other and
with other molecules in the cell.

The various non-covalent interactions can be classified as:

Ionic interactions
Van der waals interactions
Hydrogen bonds
Hydrophobic interactions

Ionic interactions
We all know and love the Coulomb force which two charges q1 and q2, separated by a distance r,
exert on each other. These charges can be located on the subunits of the biomolecules, or they
can be free ions moving in solution.

The Coulomb force is given by where k is a constant , in

vacuum, where = 8.85x1012 C2/N.m2 is the permittivity of free space. (k = 9x109 N.m2/C2).
The potential energy U of two charges is defined as the work required to bring the two charges to
a distance r apart if they are initially infinitely far away:
The potential energy is negative when the force is attractive (q1 and q2 have opposite signs), and
positive when the force is repulsive. The gradient of the potential energy function is a measure of
the force: or, more generally, .

The potential energy for the simple Coulomb interaction falls off rather gradually, as 1/r,
and hence it is also referred to as a long-range interaction.

In vacuum, U ~ 30 kBT for two charges q1 = q2 = e (1.6x1019C) separated by r ~ 2nm.

In water, which is the appropriate medium inside the cells, the Coulomb interactions are
reduced by a factor which is equal to the dielectric constant of water. Water molecules have a
permanent dipole; they align in the direction of the local electric field and effectively screen the
charges.

The dielectric constant of bulk water is 80 at room temperature.

Therefore, in water, U ~ 0.4 kBT for two ions carrying unit charges separated by ~ 2 nm.

Distance dependence of the apparent dielectric constant

The screening property from aligned dipoles is expected to decrease as the distance between the
two ions decreases, and in the limit that the two ions are right next to each other, the apparent
dielectric constant is 1. The following graph gives an empirical estimate of the apparent
dielectric constant of water as a function of the distance from an ion:

At a distance of r = 0.5 nm, the apparent dielectric constant is ~ 20, and the potential energy of
two unit charges is U 5 kBT. For decreasing value of r, the potential energy U increases both
because of the 1/r dependence as well as a smaller value for the apparent dielectric constant.
There is another very important screening effect that arises from free ions in solution and which
will cluster around charged objects (thus the name counter-ions) and further reduce the strength
and range of the Coulomb interactions. These counter-ions can be associated with the charged
objects with energies in excess of 5 kBT and hence are not easily shaken off by thermal energy.

Charge-dipole and dipole-dipole interactions

Many molecules are electrically neutral but have a permanent dipole because of an asymmetric
distribution of the electron cloud around the positively charged nuclei. For example, in HCl, the
valence electron of the H atom is donated to the Cl atom, with H carrying a net positive charge,
and Cl a net negative charge. Similarly, water has a permanent dipole because the electron
density is greater near the more electronegative O atom.

The dipole moment is defined as where d is the separation between 2 charges +q and
q. p is a vector and points in the direction from q to +q. When a molecule with a dipole moment

p is placed in an electric field E, the dipole has a potential energy

where is the angle between the vectors p and E.

Charge-dipole interactions

The electric field from a single point charge at a distance r from the charge is , and
the electric field vector points away from the charge (for positive charges) and toward the charge
(for negative charges).

The potential energy of a charge-dipole system is . The potential energy now

falls off as 1/r2, more rapidly than the charge-charge system. In the absence of thermal motion,
the dipole will align with the E field, which corresponds to =0.
Thermal averaging

Because of random collisions with the molecules of the surrounding medium, the dipole will
undergo Brownian motion. Here we will consider only the change in the orientation of the dipole
as a result of random collisions, and write down the Boltzmann probability that the dipole makes
an angle with the E field as:

Probability

The average value of the potential energy, averaged over all possible orientations whose
probability is given by the Boltzmann distribution, can be written as

where Z is the normalization constant, ,

and is the incremental solid angle between two cones swept by the p vector as it
makes an angle and with respect to the E vector.

You should be able to work out the integrals and show that

which, in the limit pU << kBT, simplifies to

Substituting for the electric field due to a point charge q at a distance r from the charge, we get

With thermal averaging, the charge-dipole interaction falls off as 1/r4.

The minus sign indicates that the interaction is always attractive.

Dipole-dipole interactions

The interaction energies between two dipoles p1 and p2 have a more complicated angular-
dependence, since there are now two dipoles, each one of which can be oriented in any direction.
Here we will write down the form of the solution without worrying about the details of the
calculations.

The potential energy has the form

where E1 is the electric field from dipole p1and depends on the angular
position of p2 relative to p1 and their relative orientations.

The distance dependence 1/r3 comes from the radial dependence of the electric field E1 of
dipole p1.

The thermal averaging with Boltzmann probabilities, in the limit U << kBT, gives:

Note that the potential energy between two dipoles falls off as 1/r6 power.

Dipole-dipole interactions are short-range interactions

Van der waals interactions

Perhaps the most important class of dipole-dipole interactions are the ones where one or both
molecules do not have a permanent dipole.

These interactions are valid for any two atoms that come into close contact with each other, and
are called Van der Waals interactions.

Dipole-induced dipole interactions

A molecule with a permanent dipole p1 can induce a dipole in another polarizable molecule. In
this case the induced dipole moment p2* points in the same direction as the inducing electric
field E1. The potential energy of interaction between p1 and p2* takes the form

where the minus sign indicates that the interaction is always attractive, since the induced dipole
always follows the direction of the instantaneous electric field. defines the angular position of
p2* relative to p1and the electric field E1 is independent of the azimuthal angle .

The magnitude of p2* depends upon the strength of the electric field at position

, where is the polarizability of the second

molecule. The interaction potential is given by:

where again we have a 1/r6 dependence.

The above result is in the absence of thermal averaging.

Thermal averaging

Since p2*, in this case, always follows the instantaneous direction of the electric field E1, thermal
averaging requires that we simply average over the dependence, with all orientations of p1

equally likely. The average value gives a numerical constant.

The average potential energy has a 1/r6 dependence as in the thermally averaged
dipole-dipole case.
Induced dipole-induced dipole interactions

A fluctuating electric field environment around each atom induces a fluctuation dipole moment
that is proportional to the polarizability of the atom. This instantaneous dipole can then induce a
dipole in a neighboring atom, resulting in an attractive potential that also has a 1/r6
dependence.

Short-range repulsive interaction

As the atoms get too close, at some point there is a strong repulsion from overlapping electron
clouds and Paulis exclusion principle whereby filled electron shells of an atom cannot
accommodate any more electrons.

Lennard-Jones potential

A commonly used analytical form that lumps together all dipole-dipole interactions and includes
both the attractive and the repulsive terms is the Lennard-Jones potential where the repulsive
term is approximated as having a 1/r12 dependence:

This form of the potential energy function has a minimum at r = ro with .

The atoms can be treated as spheres defined by a Van der Waals radius that is a measure of how
close another atoms can come before a strong, very short range, repulsive force kicks in.

Some typical Van der Waals radii of atoms are hydrogen ~ 1.2 A , oxygen ~ 1.4 A , nitrogen ~
1.6 A , and carbon ~ 2 A .
Hydrogen bonds
A very important interaction responsible for the structure and properties of water, as well as the
structure and properties of biological macromolecules, is the hydrogen bond.

A hydrogen bond is an interaction between a proton donor group D-H and a proton acceptor
atom A.

D-H is stongly polar, which means that the electron density is primarily around the
electronegative atom (examples, F-H, O-H, N-H, S-H in order of decreasing polarity). The
acceptor atom A is also strongly electronegative.

The hydrogen bond interaction is more than just an ionic or dipole-dipole interaction between the
donor and the acceptor groups. The distance between the H and A in a hydrogen bond is less
than the sum of their respective Van der Waals radii.

Hydrogen bonds are usually shown as although the strength of the

interaction can sometimes be as strong as . The hydrogen bond is strongest
when the three atoms D, H, and A have a collinear geometry. The strength of the hydrogen bonds
in biological macromolecules ranges from ~ 2 kBT to ~ 5kBT.

Hydrogen bonding network in water

Hydrophobic interactions
Another very important interaction is the hydrophobic interaction. As the term hydrophobic
suggests, this interaction is an effective interaction between two nonpolar molecules that tend to
avoid water and, as a result, prefer to cluster around each other.
Unlike all the other interactions that we have studied so far and which are pairwise interactions
between atoms or parts of molecules, the nature of the hydrophobic interaction is very different.
It involves a considerable number of (water) molecules, and does not arise as a result of a direct
force between the nonpolar molecules.

Nonpolar molecules are not good acceptors of the hydrogen bond. When a nonpolar molecule is
placed in water, the hydrogen bonding network of water is disrupted. The water molecules
therefore reorganize around the solute and make a sort of cage, similar to the structure of water
in ice, in order to gain back the broken hydrogen bonds. This reorganization results in a
considerable loss in the configurational entropy of water and therefore an increase in the free
energy G.

If there are two or more such nonpolar molecules, the configuration in which they are spatially
together (clustered together) is preferred because now the hydrogen bonding network of water is
disrupted in one (albeit bigger) pocket, rather than in several small pockets. Therefore, the
entropy of water is larger when the nonpolar molecules are clustered together, leading to a
decrease in the free energy.

At equilibrium, the configuration with the lower free energy and which has a higher Boltzmann
probability, is the preferred configuration.

Hydrophobic interactions have strengths of a few kBT and are comparable in energy to hydrogen
bonds.

Screening of Electrostatic Interactions

Interactions between charges relevant in biology are almost always affected - and usually
reduced in strength or screened - by the presence of many nearby water molecules, ions, and
other molecules.

Unscreened (Vacuum) Coulomb Interaction

We all know that in vacuum, two charges q1 and q2 separated by a distance r have a Coulomb
interaction energy of

kq1 q2
U(r) =
r
9 2 2
where k = 1/(40) = 8.99 10 Nm /C .

We call this a long-ranged interaction because of its slow power-law decay. In vacuum, the field
lines starting out from an isolated charge flow off to infinity without terminating.
Essentially all interactions relevant to biology boil down to superposition of a lot of fundamental
Coulomb interactions. But it is extremely impractical to think in terms of fundamental
interactions when thinking about molecules in liquid water.

Dipoles in Polarizable Media Reduce The Strength of the Coulomb Interaction

We learned in electrostatics that charges embedded in a dielectric material interact by a Coulomb

interaction which is reduced in strength by a dimensionless factor called the dielectric constant :

k q1 q2
U(r) =
r
This reduction in strength of the Coulomb interaction is due to the polarization of the particles of
the dielectric medium - either induced or permanent dipoles around a free charge will be oriented
so as to terminate some of the field lines coming from the free charge.

Note that the Coulomb interaction continues to have its long-ranged character, just with a
reduced strength. This is sometimes referred to as dielectric screening of the charge.

For pure water at room pressure and 25 C, = 78.5, i.e. Coulomb interactions are reduced in
strength by a factor of about 80 relative to the vacuum. This is because of the permanent dipole
moment carried by every water molecule. Note that the electrons tend to stay close to the
oxygen, leaving two positively charged protons on one side of an H2O.

Sometimes people refer to this reduction of the strength of the Coulomb interaction as
`screening' of the charge.

Example: Estimate the range at which two electron charges have an interaction energy kB T, in
pure water at standard lab pressure and temperature.

kB T = k q1 q2 / (r) or r = k e2 / (kB T)

Plug in k = 9109 Nm2/C2, e = 1.61019 C, = 80, and kB T = 41021 J, to find r = 71010 m

=7

This distance is often called the Bjerrum length

k e2
lB = = 7 = 0.7 nm
kB T