Biology Reference
In-Depth Information
variety of disciplines aiming to survey and understand the proteome falls
under the umbrella of proteomics.
The complexity of studying the proteome arises from the fact
that proteins encoded by genes can undergo a number of processing
events that are regulated in space and time. Although a particular
organism is endowed with a single genome, there are several corre-
sponding proteomes for each cell population at a certain time and under
specific environmental influences. At the molecular level, a single
gene encoding a protein yields a product that is then processed and
modified (e.g. glycosylation or phosphorylation), amplifying the vari-
ants. Thus the estimated 25 000 genes in humans, for example, get
amplified to more than a million protein species (Cho, 2007; Kosak
et al
., 2004).
Techniques and strategies
Given the above numbers, it seems almost impossible to make sense of
the proteome. Fortunately the methods used to address issues in pro-
teomics simplify the existing variation into more manageable magnitudes
because the techniques offer the possibility for efficient profiling. There is
no immediate need to account for all minor differences allowing a survey,
for example, of relevant proteins that may fluctuate as a result of a certain
disease.
The techniques involved in proteomics include those which can be
used for protein separation, identification and quantification. More
advanced applications allow for structural analysis, identifying/mapping
modifications, defining complex interactions and even tracking protein
regulation in the cellular context. One of the most common strategies
include one-dimensional (1D) and two-dimensional (2D) gel electro-
phoresis, various types of chromatography, and mass spectrometry (Link,
2002). The latter is powerful as a stand-alone technique in proteomics
research but maximal effectiveness is achieved when it is coupled to the
above-mentioned separation methods.
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