In
a short year, proteomics, the systemic study of proteins based on
the genome, has captured the attention of academia, government and
industry alike. This dramatic new focus was clearly discernable
from the presentations at a recent symposium organized by the National
Academies (Defining the Mandate of Proteomics in the Post-Genomics
Era) as well as from the January 2002 launching of two new dedicated
journals (Journal of Proteome Research by the American Chemical
Society and Molecular and Cellular Proteomics by the American Society
for Biochemistry & Molecular Biology). According to current
estimates, the 3 billion base pairs in the human genome only code
for approximately 30,000 genes. During the life cycle of cells,
the information in these genes is translated into proteins, the
real actors in cellular processes. The proteins in turn perform
the necessary tasks (signaling, regulation, catalysis, etc.) that
keep the cells alive. Throughout these processes, the proteins undergo
posttranslational modifications that significantly alter their structure
and function. The expression level of these proteins also varies
as a function of cell type, position within the cell and phase of
cell evolution (i.e., time). Although determining the identity,
structure and concentration of the significant proteins is a daunting
task, the potential return of this endeavor is hard to resist. On
the scholarly level, one can expect to gain a vastly improved understanding
of life as it is reflected in the cell cycle. On a practical level,
this understanding enables the design of smart drugs that specifically
target the cellular process related to a particular disease. Current
developments in analytical instrumentation, more specifically mass
spectrometry, have led to the technology that enables the high throughput
protein analysis that is a prerequisite for answering the questions
posed by proteomics. Due to the high efficiency of biomolecules
in performing their tasks, some of them are present in the cells
at very low concentrations. (For example, only a few hundred molecules
of some of the signaling proteins are present in any given cell).
Determining the identity, primary structure and concentration of
these species is a significant challenge. Matrix-assisted laser
desorption ionization (MALDI) and electrospray ionization (ESI)
mass spectrometry (MS) are indispensable tools in the quest for
this information. This month, the 2002 Nobel Prize in Chemistry
was awarded for the discovery of these methods.
In
a short year, proteomics, the systemic study of proteins based on
the genome, has captured the attention of academia, government and
industry alike. This dramatic new focus was clearly discernable
from the presentations at a recent symposium organized by the National
Academies (Defining the Mandate of Proteomics in the Post-Genomics
Era) as well as from the January 2002 launching of two new dedicated
journals (Journal of Proteome Research by the American Chemical
Society and Molecular and Cellular Proteomics by the American Society
for Biochemistry & Molecular Biology). According to current
estimates, the 3 billion base pairs in the human genome only code
for approximately 30,000 genes. During the life cycle of cells,
the information in these genes is translated into proteins, the
real actors in cellular processes. The proteins in turn perform
the necessary tasks (signaling, regulation, catalysis, etc.) that
keep the cells alive. Throughout these processes, the proteins undergo
posttranslational modifications that significantly alter their structure
and function. The expression level of these proteins also varies
as a function of cell type, position within the cell and phase of
cell evolution (i.e., time). Although determining the identity,
structure and concentration of the significant proteins is a daunting
task, the potential return of this endeavor is hard to resist. On
the scholarly level, one can expect to gain a vastly improved understanding
of life as it is reflected in the cell cycle. On a practical level,
this understanding enables the design of smart drugs that specifically
target the cellular process related to a particular disease. Current
developments in analytical instrumentation, more specifically mass
spectrometry, have led to the technology that enables the high throughput
protein analysis that is a prerequisite for answering the questions
posed by proteomics. Due to the high efficiency of biomolecules
in performing their tasks, some of them are present in the cells
at very low concentrations. (For example, only a few hundred molecules
of some of the signaling proteins are present in any given cell).
Determining the identity, primary structure and concentration of
these species is a significant challenge. Matrix-assisted laser
desorption ionization (MALDI) and electrospray ionization (ESI)
mass spectrometry (MS) are indispensable tools in the quest for
this information. This month, the 2002 Nobel Prize in Chemistry
was awarded for the discovery of these methods. 