Chapter 8 – Theoretical Biophysics  377

Defining C(x0,y0,z0) as a numerical convolution integral and also comprising the Gaussian

excitation field dependence over a cell, and assuming the time-​averaged dye density is uni­

form in space, we can calculate the dye density, in the case of a simple single internal cellular

compartment, as

(8.123)

ρ = (

)

(

)

=

(

)

+

(

)

I x y z

A

C x y z

I

I

x y z

I

I

C x y z

0

0

0

0

0

0

0

0

0

0

0

0

,

,

,

,

,

,

,

,

d

s

a

d

((

)Is

The mean value of the total background noise (Ia +​ Id) can usually be calculated from parental

cells that do not contain any foreign fluorescent dye tags. In a more general case of several

different internal cellular compartments, this model can be extended:

(8.124) I x y z

A

I

x

y

xy

j

Number of

comp

0

0

0

2

2

1

2

,

,

(

)

=

+

=

d

exp

s

σ

artments

i

Compartment

voxels

j

i

i

i

P x

x y

y z

z

=

(

)

1

0

0

0

ρ

,

,

where ρj is the mean concentration of the jth compartment, which can be estimated from this

equation by least squares analysis. An important feature of this model is that each separate

compartment does not necessarily have to be modeled by a simple geometrical shape (such

as a sphere) but can be any enclosed 3D volume provided its boundaries are well-​defined to

allow numerical integration.

Distributions of copy numbers can be rendered using objective KDE analysis similar to

that used for stoichiometry estimation in distinct fluorescent spots. The number of protein

molecules per cell has a typically asymmetrical distribution that could be fitted well using a

random telegraph model for gene expression that results in a gamma probability distribution

p(x) that has similarities to a Gaussian distribution but possesses an elongated tail region:

(8.125)

p x

x

x b

b

a

a

a

( ) =

(

)

( )

1exp

/

Γ

where Γ(a) is a gamma function with parameters a and b determined from the two moments

of the gamma distribution by its mean value m and standard deviation, such that a =​ m2/​σ2

and b =​ σ2/​m.

8.5.5  BIOINFORMATICS TOOLS

Several valuable computational bioinformatics tools are available, many developed

by the academic community and open source, which can be used to investigate pro­

tein structures and nucleotide sequences of nucleic acid, for example, to probe for the

appearance of the same sequence repeat in different sets of proteins or to predict sec­

ondary structures from the primary sequences. These algorithms operate on the basis

that amino acids can be pooled in different classes according to their physical and chem­

ical properties (see Chapter 2). Thus, to some extent, there is interchangeability between

amino acids within the same class such that an ultimate secondary, tertiary, and quater­

nary structure may be similar. These tools are also trained using predetermined struc­

tural data from EM, NMR, and x-​ray diffraction methods (see Chapter 5), enabling likely

structural motifs to be identified from their raw sequence data alone. The most common

algorithm used is the basic alignment search tool (BLAST).

Homology modeling (also known as comparative modeling) is a bioinformatics tool for

determining atomic-​level resolution molecular structures. It is most commonly performed

on proteins operating by interpolating a sequence, usually the primary structure of amino