The cell (from Latin cella, meaning "small room") chloroplast.
plast. Each is separated from the rest of the cell by
is the basic structural, functional, and biological unit of
all known organisms. A cell is the smallest unit of life.
Cells are often called the "building blocks of life". The
study of cells is called cell biology, cellular biology, or
cytology.
Cells consist of cytoplasm enclosed within a
membrane, which contains many biomolecules such
as proteins and nucleic acids. Most plant and animal
cells are only visible under a microscope, with
dimensions between 1 and 100 micrometers.
Organisms can be classified as unicellular (consisting
of a single cell such as bacteria) or multicellular
(including plants and animals). Most unicellular
organisms are classed as microorganisms.
Cells are of two types: eukaryotic, which contains
a nucleus, and prokaryotic, which do not. Prokaryotes
are single-celled organisms, while eukaryotes can be
either single-celled or multicellular.
Biochemistry and the Organization of Cells
Biochemistry describes the molecular nature of life
processes. In living cells, many chemical reactions take
place simultaneously.
Cells of all types have so many fundamental features
in common that it is reasonable to say that they all
had a common origin.
Life is based on compounds of carbon. This is the
subject matter of organic chemistry.
The reactions of organic compounds are those of
their functional groups, which are specifically linked
atoms that react in similar ways under many different
conditions. Our solar system, including the Earth, is
postulated to have been formed from chemical
elements produced by first-generation stars. The early
Earth had an atmosphere that consisted of simple
chemical compounds.
The atmospheric conditions of the early Earth
allowed the formation of molecules, such as amino
acids, that play a role in life processes.
Several theories describe the origin of living cells
from component molecules. All require explanations
for coding and for catalytic activity, and all assign an
important role to RNA.
All cells contain DNA and are separated from their
environment by a cell membrane. Prokaryotic cells do
not have significant internal membranes, but the
larger cells of eukaryotes have an extensive
membrane system. The internal membranes mark off
the organelles, portions of the cell with a specific
function.
Prokaryotes have a nuclear region, which contains
DNA, and ribosomes, the site of protein synthesis, as
their main features. They have a cell membrane but
do not have an internal membrane system.
Three of the most important organelles in eukaryotic
cells are the nucleus, the mitochondrion, and the
a double membrane. The nucleus contains most of the
DNA of the cell and is the site of RNA synthesis. The
mitochondria contain enzymes that catalyze important
energy-yielding reactions.
Chloroplasts, which are found in green plants and green
algae, are the sites of photosynthesis. Both mitochondria
and chloroplasts contain DNA that differs from that found
in the nucleus, and both carry out transcription and
protein synthesis distinct from that directed by the
nucleus.
Other organelles play specific roles. They include the
Golgi apparatus, lysosomes, and peroxisomes.
In the five-kingdom classification scheme, prokaryotes
have a kingdom to themselves (Monera). The remaining
four kingdoms – protists, fungi, plants, and animals –
consist of eukaryotes.
In the three-domain classification schemes, eukaryotes
have a domain to themselves. Two domains consist of
prokaryotes. Eubacteria are the commonly encountered
prokaryotes. Archaea are organisms that live in extreme
environments such as those that were found on the early
Earth.
Many theories about the rise of eukaryotes from
prokaryotes focus on a possible role for symbiosis.
The idea of endosymbiosis, in which a larger cell engulfs
a smaller one, plays a large role in scenarios for the
development of organelles in eukaryotic cells.
The sun is the source of energy for all life on Earth. It
provides the energy for photosynthesis, which produces
carbohydrates as well as oxygen. Carbohydrates can be
processed in chemical reactions that release energy.
Reactions that release energy are favored and thus are
likely to occur. Thermodynamics is the branch of science
that predicts the likelihood of reactions.
A spontaneous reaction is one that will take place
without outside intervention. This point does not specify
the reaction rate. Some spontaneous processes can take a
long time to occur.
The change in free energy (ΔG) that accompanies a
reaction determines whether that reaction is spontaneous
at a given temperature and pressure.
A negative free energy change (ΔG<0) is characteristic of
a spontaneous reaction. A positive free energy change
(ΔG>0) indicates that the reaction is not spontaneous, but
the reverse process is spontaneous. When the free energy
change is zero (ΔG = 0), the reaction is at equilibrium.
Living things are ordered assemblies of molecules. They
represent a local decrease in entropy. Because the
entropy of the universe increases in spontaneous
processes, this local decrease in entropy is offset by a
larger increase in the entropy of the surroundings. There
is an increase in total entropy.
 Water is tasteless, odorless, and The three-dimensional structures of many
transparent. In small quantities, it is also important biomolecules, including proteins and
colorless. Water is capable of dissolving a nucleic acids, are stabilized by hydrogen bonds.
variety of different substances, which is why Acids are proton donors, and bases are proton
it is such a good solvent. And, water is called acceptors.
the "universal solvent" because it dissolves Water can accept or donate protons.
more substances than any other liquid. The strength of an acid is measured by its acid
This allows the water molecule to dissociation constant, Ka. The larger the Ka, the
become attracted to many other different stronger the acid and the more H+ dissociates.
types of molecules. Water molecules are The concentration of H+ is expressed
polar, so they form hydrogen bonds. This conveniently as the pH, which is the negative
gives water unique properties, such as a log of the hydrogen ion concentration.
relatively high boiling point, high specific A similar expression, pKa, can be used in place
heat, cohesion, adhesion, and density. Water of the Ka. pKa = -log Ka.
is directly involved in many chemical
The pH of a solution of a weak acid and its
reactions to build and break down important
conjugate base is related to the concentration of
components of the cell. Conversely, water is
the acid and base and the pKa by the Henderson-
required for the reverse reaction that breaks
Hasselbalch equation.
down these molecules, allowing cells to
In aqueous solution, the relative concentrations
obtain nutrients or repurpose pieces of big
of a weak acid and its conjugate base can be
molecules.
related to the titration curve of the acid.
Water: The Solvent for Biochemical
Reactions In the region of the titration curve in which the
pH changes very little upon addition of aid or
Water is a polar molecule, with a partial
base, the acid/base ratio varies within a narrow
negative charge on the oxygen and partial
range (10:1 at one extreme and 1:10 at the other
positive charges on the hydrogens.
extreme).
There are forces of attraction between the
Buffer solutions are characterized by their
unlike charges.
tendency to resist pH change when small
Polar substances tend to dissolve in water,
amounts of strong acid or strong base are added.
but nonpolar substances do not.
Buffers work because the concentration of the
The properties of water have a direct effect
weak acid and base is kept in the narrow
on the behavior of biomolecules.
window of the acid titration curve.
There are several different types of forces
Many experiments must have a buffered
based on the charge that will be seen
system to keep a stable pH.
frequently. These include, from strongest to
There are many physiological buffers, such as
weakest, ionic bonds, ion-dipole bonds,
dipole-dipole bonds, dipole-induced dipole the bicarbonate blood buffer or the phosphate
bonds, induced dipole-induced dipole bonds. buffer that help maintain physiological pH.
A hydrogen bond is a special example of a
dipole-dipole bond.
Water molecules are extensively hydrogen-
bonded.
The ability to form strong hydrogen bonds
is responsible for the many unique
characteristics of water, such as its very high
melting point and boiling point for a
molecule of its size.
 The central dogma of molecular biology describes
the flow of genetic information in cells from DNA to
messenger RNA (mRNA) to protein. It states that genes
specify the sequence of mRNA molecules, which in turn
specify the sequence of proteins. Information from a gene is
used to build a functional product in a process called gene
expression. A gene that encodes a polypeptide is expressed in
two steps. In this process, information flows from DNA →
RNA → protein, a directional relationship known as the
central dogma of molecular biology.
Genetic information is passed from generation to
generation through inherited units of chemical information (in
most cases, genes). Organisms produce other similar
organisms through sexual reproduction, which allows the line
of genetic material to be maintained and generations to be
linked.
Transcription of the Genetic Code: Biosynthesis of RNA
Transcription is the process of using a DNA template to
produce RNA
There are many types of RNA produced, such as messenger
RNA, transfer RNA, ribosomal RNA, micro RNA, small
interfering RNA, and small nuclear RNA.
A primer is not needed for RNA synthesis
As does all polynucleotide synthesis, the reaction proceeds
in the 5’ to 3’ direction.
Prokaryotic transcription is catalyzed by RNA polymerase,
which is a 470,000 Dalton enzyme with 5 types of subunits.
RNA polymerase moves along the template strand of DNA
and produces a complementary RNA sequence that matches
the coding strand of DNA.
RNA Polymerase recognizes specific DNA sequences called
promoters and binds to the DNA. The promoters tell the
polymerase which DNA should be transcribed.
The  subunit is loosely bound to RNA polymerase and is
involved in promoter recognition.
Transcription can be divided into three parts – initiation,
elongation, and termination.
There are four principal control mechanisms for prokaryotic
transcription – alternative factors, enhancers, operons, and
transcription attenuation.
Alternative  factors can direct RNA polymerase to
different promoters, altering the choice of RNA product.
Enhancers and silencers are DNA sequences usually found
upstream of promoters that stimulate or reduce transcription,
respectively. These sequences bind to specific proteins called
transcription factors.
Operons are groups of genes involved in a common
metabolic process that are controlled as a group. A common
example is the lac operon that produces -galactosidase and
other enzymes involved in metabolism of lactose.
With an operon, a regulatory gene produces either an
inducer or a repressor of the operon. A metabolite acts as a
co-inducer or co-repressor to affect the transcription of the
structural genes.
Transcription attenuation controls transcription after it has
begun by adjusting the level of transcription based on the
quantity of a related metabolite. For example, in the trp
operon, the level of tryptophan affects the transcription of the
genes that produce the enzymes that make tryptophan.
Eukaryotic transcription is far more complicated than the
prokaryotic version.
There are 3 principal RNA polymerases in eukaryotes, of
which Pol II produces mRNA.
Pol II is a large protein with at least 12 subunits. Some of
the subunits share homology with the subunits of prokaryotic
RNA Polymerase as well as with eukaryotic Pol I and Pol III.
The organization of promoters and enhancers is more
complicated with eukaryotes. An important promoter element is
the TATA box at -25.
Initiation of eukaryotic transcription is also much more
complicated. In addition to the polymerase and the promoter,
there are 6 general transcription factors involved in forming the
initiation complex.
Two other RNA polymerases, pol IV and V, are poorly
understood but are involved in producing small non-coding
RNA’s.
Control of eukaryotic transcription includes many of the same
concepts seen with prokaryotic transcription.
The use of enhancers and silencers is more extensive and the
promoters are more complicated.
A protein called Mediator is involved in activation of
transcription. Mediator bridges the promoter region and specific
enhancers or silencers.
Activation of eukaryotic transcription is also based on the
repression of transcription caused by chromatin structure. The
chromatin must be relaxed in order for polymerase to access the
DNA.
Chromatin remodeling complexes and histone-modifying
enzymes are involved in the relaxation of the chromatin.
Histones and DNA are modified by methylation,
phosphorylation, ubiquitinylation, and acetylation.
Many control mechanisms are based on response elements,
enhancers that respond to some metabolic signal, like heat, heavy
metals, or other specific molecules such as cAMP.
One very important response element is the cyclic AMP
response element (CRE). A specific transcription factor called
CREB and a mediating protein called CBP are involved in many
metabolic processes in eukaryotes.
Most of the transcription of DNA to RNA does not lead to
RNA’s that code for proteins, rather it leads to non-coding RNA
The two principal types of non-coding RNA’s are micro RNA’s
(MiRNA) and small interfering RNA’s (SiRNA)
Micro RNAs are about 22 nucleotides long, and are cut from a
longer, hairpin-shaped RNA by the enzyme Dicer. MiRNAs bind
imperfectly to specific mRNAs and block their transcription.
Biosynthesis of RNA 3
SiRNAs are formed in a way similar to miRNA, by the enzyme
Dicer. When a cell detects specific double-stranded RNA
molecules, Dicer cuts them into small pieces of 21–25
nucleotides. These then bind to mRNA molecules in the process
known as RNA interference (RNAi), targeting them for
destruction.
Proteins such as transcription factors that bind to DNA often
have recognizable structural motifs.
Common motifs are the helix-turn-helix, zinc fingers, and basic-
region leucine zippers.
The fact that many transcription factors and other DNA binding
proteins have such motifs has aided in the identification of these
proteins when they are initially discovered.
In addition to binding DNA, many proteins involved in
transcription bind to other proteins.
Many protein-protein binding domains also have identifiable
motifs, such as acidic domains, glutamine-rich domains, and
proline-rich domains.
After being transcribed from DNA, many RNA molecules are
modified, often extensively, before they arrive at their final form.
Several modifications are common with tRNA and rRNA, such
as trimming, the addition of terminal sequences, and base
modification.
Messenger RNA is modified by putting a cap on the 5’ end and a
poly-A tail on the 3’ end.
Messenger RNA is also modified by the removal of
intervening sequences, or introns.
The reaction that removes introns involves the formation of
a lariat as an intermediate. Splicing also depends on a
separate type of RNA called a small nuclear
ribonucleoprotein, or snRNP (pronounced snurp).
Alternative splicing of mRNA helps account for the fact that
there are more proteins produced in eukaryotes than there are
separate genes.
Proteins are not the only biological molecules with catalytic
properties. Some RNAs, called ribozymes, also catalyze
certain reactions.
Group I ribozymes require an external guanosine for
reactivity. Group II ribozymes do.
Protein Synthesis: Translation of the Genetic Message
Protein translation involves 3 types of RNA and many
protein factors.
Amino acids are activated via enzymes called aminoacyl-
tRNA synthetases.
The formation of a protein takes place in four steps called
activation, initiation, elongation, and termination.
The genetic code is based on a series of three bases coding
for an amino acid.
The code is nearly universal in all organisms from viruses
through humans. The code has no punctuation, meaning the
mRNA is read three bases at a time with no spaces in
between. The code is non-overlapping as well, meaning that
each base is part of only one codon.
The genetic code was determined by a variety of techniques,
such as using synthetic mRNA with known sequences to see
what proteins would be translated from them.
While there are 64 combinations of three bases leading to 64
codons, there are fewer types of tRNA anticodons. This
means that standard Watson-Crick base pairing must be
broken on occasion. The wobble model of codon-anticodon
base pairing shows that some bases at the 5’ end of the
anticodon of the tRNA can base pair with multiple bases on
the codon.
While there may be many codons for a particular amino
acid, not all potential codons are represented equally.
Before amino acids can be incorporated into a peptide, they
must be activated.
Amino acids are activated through a reaction with ATP
yielding an amino acid bonded to AMP. The AMP-bound
amino acid is then reacted with a tRNA to yield an aminoacyl
tRNA.
The enzymes responsible for activation are called
aminoacyl-tRNA synthetases.
The unique and elegant structure of the ribosome allows the
binding of aminoacyl-tRNA molecules and mRNA. The
ribosome catalyzes the nucleophilic attack of one amino acid
upon the next, allowing for protein synthesis
Protein synthesis begins at an AUG codon on the mRNA.
The ribosome and mRNA forms an initiation complex that
includes the two main ribosomal subunits, the mRNA, GTP,
and three initiation factors, IF1, IF2, and IF3.
The ribosome locates the correct AUG to start translation by
binding to a consensus sequence called the Shine-Dalgarno
sequence.
The first aminoacyl-tRNA bound to the ribosome carries N-
formyl-methionine, and it is initially bound to the P-site of
the ribosome.
In chain elongation, the second amino acyl-tRNA binds to
the A-site. This amino acid’s -amino group performs a
nucleophilic attack on the carbonyl group of the N-formyl-
methionine in the peptidyl transfer reaction. In a translocation
step, the ribosome then moves one codon leaving a dipeptidyl-
tRNA in the A-site and moving the uncharged tRNA to the exit
site. The components continues with a new aminoacyl-tRNA
entering the P-site. The uncharged tRNA is then ejected from the
E-site.
When the ribosome encounters a stop codon, the chain is
terminated in a process requiring GTP and three protein release
factors.
The ribosome is actually a ribozyme. There are no amino acids
at the active site where the peptidyl transferase reaction occurs.
Specific bases on the rRNA are believed to catalyze the reaction.
Eukaryotic translation involves many more protein factors than
the corresponding translation in prokaryotes
Both the 5’-Cap and the 3’ poly-A tail are involved in orienting
the ribosome close to the correct AUG used as the start codon.
There is no Shine-Dalgarno sequence in eukaryotic mRNA.
Once bound, the ribosome moves down the mRNA scanning for
the correct AUG until it finds one that is in the correct context,
which is identified by a small mRNA sequence around the AUG
is called a Kozak sequence.
Eukaryotic chain elongation is similar to the prokaryotic
counterpart. With chain termination, there is only one release
factor that binds to all three stop codons.
It has recently been found that there is some coupled
transcription and translation in the nucleus of eukaryotic cells.
It has also been recently found that in certain circumstances
found in the immune system, AUG is not the start codon, rather
CUG, leaving leucine as the N-terminal amino acid.
Proteins are usually modified after their initial translation.
Protein modification includes removal of the N-formyl-
methionine from prokaryotic proteins, cleavage of specific amino
acids, and addition of signal sequences.
Non-protein components can be added to some proteins, such as
the heme group added to hemoglobin.
Proteins must also be folded properly into their correct form.
Protein molecules called chaperones help many proteins fold into
their correct form.
It was recently found that in some cases, the ribosome itself acts
as its own chaperone and that proteins translated apart from
ribosomes fold differently than proteins translated with
ribosomes.
Proteins are degraded in subcellular organelles, such as
lysosomes, or in macromolecular structures called proteasomes.
Many proteins are targeted for destruction by being bound to a
protein called ubiquitin.
The nature of the amino acid sequence at the N-terminus is often
very important to control of the timing of the destruction of a
protein.
 Nucleic acid is an important class of
macromolecules found in all cells and viruses. The
functions of nucleic acids have to do with the
storage and expression of genetic information.
Deoxyribonucleic acid (DNA) encodes the
information the cell needs to make proteins. A
related type of nucleic acid, called ribonucleic acid
(RNA), comes in different molecular forms that
participate in protein synthesis. Nucleic acids are
long chainlike molecules composed of a series of
nearly identical building blocks called nucleotides.
Each nucleotide consists of a nitrogen-
containing aromatic base attached to a pentose (five-
carbon) sugar, which is in turn attached to a
phosphate group. A nucleotide is made up of three
components: a nitrogenous base, a pentose sugar,
and a phosphate group. The two main types of
nucleic acids are deoxyribonucleic acid (DNA) and
ribonucleic acid (RNA).
Nucleic Acids: How Structure Conveys Information
The two principal kinds of nucleic acids are DNA
and RNA. The primary structure of nucleic acids is
the order of bases. The secondary structure is the
three-dimensional conformation of the backbone.
The tertiary structure is the supercoiling of the
molecule.
Two kinds of nitrogen-containing nucleobases,
pyrimidines and purines, are joined to sugars to
form nucleosides.
The sugar is deoxyribose in DNA and ribose in
RNA.
The addition of phosphate groups to nucleotides
gives rise to nucleotides, which are the monomers of
nucleic acids.
When nucleotides are joined by phosphodiester
bonds, they form a sugar-phosphate backbone,
giving rise to DNA and RNA.
The sequence of bases is a very important feature
of the primary structure of nucleic acids because the
sequence is the genetic information that ultimately
leads to the sequence of RNA and protein.
The double helix is the predominant secondary
structure of DNA. The sugar–phosphate backbones,
which run in antiparallel directions on the two
strands, lie on the outside of the helix. Pairs of
bases, one on each strand, are held in alignment by
hydrogen bonds.
The base pairs lie in a plane perpendicular to the
helix axis in the most usual form of the double
helix, but there are variations in structure.
The tertiary structure of DNA depends on
supercoiling. In prokaryotes, the circular DNA is
twisted before the circle is sealed, giving rise to
supercoiling. In eukaryotes, the supercoiled DNA is
complexed with proteins known as histones.
The two strands of the double helix can be separated
by heating DNA samples. This process is called
denaturation. DNA denaturation can be monitored by
observing the rise in ultraviolet absorption that
accompanies the process. The temperature at which
DNA becomes denatured by heat depends on its base
composition; higher temperatures are needed to
denature DNA rich in G-C base pairs.
Four kinds of RNA—transfer RNA, ribosomal RNA,
messenger RNA, and small nuclear RNA—are involved
in protein synthesis.
Transfer RNA transports amino acids to the sites of
protein synthesis on ribosomes, hich consist of
ribosomal RNAs and proteins.
Messenger RNA directs the amino acid sequence of
proteins. Small nuclear RNA is used to help process
eukaryotic mRNA to its final form.
RNA interference, which requires short stretches of
siRNA, exerts control over gene expression. Nucleic
Acid Biotechnology Techniques
In order to study nucleic acids, we must have a way to
separate and identify them.
The most common separation technique is gel
electrophoresis. DNA pieces separate on a gel-based on
size.
DNA can be visualized on a gel via autoradiography, a
procedure where the DNA has incorporated radioactive
nucleotides.
DNA can also be seen using fluorescence, often with a
compound called ethidium bromide, which glows
orange under UV light when bound to DNA. The
disadvantage is that ethidium bromide is a strong
carcinogen.
Other dyes, such as SyBr green, that are not
carcinogenic, are now being used to avoid
environmental hazards. Restriction endonucleases are
enzymes produced by bacteria that hydrolyze the
phosphodiester backbone of DNA at specific sequences.
The sequences targeted by restriction endonucleases
are palindromes, meaning their sequence reads the same
on both strands going in the same direction.
Most restriction enzymes cut DNA in a way that
leaves sticky ends that are very useful for recombining
DNA from different sources.
Cloning refers to creating a genetically identical
population.
DNA can be combined by using restriction enzymes
that create sticky ends in the DNA. This recombinant
DNA will have a target DNA sequence that the
experimenter is interested in.
The target DNA sequence is carried in some type of
vector, usually a bacterial plasmid or a virus.
The target DNA sequence is inserted into a host
organism and the natural doubling time of the organism
is used to create many copies of the target DNA
sequence.
Those organisms that are carrying the target DNA
are identified through a process called selection.
Selection often involves antibiotic resistance.
Genetic engineering is the process of inserting
genes of interest into specific organisms for either a
medical or purely scientific benefit.
Gene therapy is the process of inserting a missing
gene into an organism.
Bacteria are often used as the factories to produce a
protein from a cloned gene. This has led to the
production of human proteins such as insulin and
erythropoietin.
To produce the protein product of a gene of
interest, the gene must be cloned into an expression
vector, usually a plasmid with special features that
allows it to be transcribed and translated in a host
cell.
In agriculture, genetic engineering is used to
produce crops that are resistant to insects or have
long shelf lives. A DNA library is a collection of
clones of an entire genome.
The genome is digested with restriction enzymes
and the pieces are cloned into vectors and
transformed into cell lines.
Specific radioactive probes to a sequence of
interest are reacted to filters that have copies of the
bacterial colonies in the library. The probe will bind
to the sequence of interest and the colony’s location
can be seen via autoradiography.
A cDNA library is constructed by using reverse
transcriptase to make DNA from the mRNA in a
cell. This cDNA is then used to construct a library
similar to a genomic DNA library.
Polymerase Chain Reaction (PCR) is a
sophisticated, automated technique for amplifying
DNA from very small amounts of samples. The
DNA to be amplified is mixed with specific primers,
dNTPs, and a heat stabile form of DNA polymerase.
The mixture undergoes 20-40 rounds of DNA
polymerization via cycling the temperatures so that
the DNA strands separate, the primers anneal, and
the polymerase fills in the DNA. Each cycle doubles
the target DNA.
The technique has revolutionized forensic science
as DNA can be amplified from just a few cells and
then the DNA is analyzed and identified
A newer PCR technique, called quantitative PCR
(qPCR) can be used to measure the original amount
of DNA in a sample being amplified.
A DNA fingerprint is created by digesting DNA
with restriction enzymes, separating the pieces on a
gel, and then visualizing some of the pieces by using
labeled probes.
Differences in DNA patterns between different
individuals are based on different base sequences of
their DNA. These base sequence differences mean there
will be different restriction sites leading to different
length fragments.
DNA can be sequenced by using several techniques.
One of the most common is called the chain termination
method.
Dideoxy nucleotides are used to terminate DNA
synthesis. Multiple reactions are run with a different
dideoxynucleotide in each reaction mix.
The reactions produce a series of DNA fragments of
different length that can be run on a gel and the
sequence determined by tracking the different length
fragments in the lanes with the 4 different
dideoxynucleotide.
As more DNA sequences become available, it
becomes possible to compare those sequences. Of
particular interest is any pattern that may emerge from
genes that encode proteins with similar functions.
Important medical applications are emerging, and new
methods are making it possible to analyze large
quantities of data. Complete protein: protein interaction
maps are now available for eukaryotes.
The proteome is the protein version of the genome. It
refers to all the proteins being expressed in a cell. The
study of proteomics is becoming very important in the
life sciences.
A very powerful technique in vogue these days is the
use of DNA or protein microchips. With these chips,
thousands of samples of DNA or proteins can be
applied and then checked for binding of biological
samples.
The binding is visualized by using fluorescently
labeled molecules and scanning the chip with a
computer. The pattern of fluorescent labels then gives
an indication of which mRNA or proteins are being
expressed in the samples.