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"Low-Abundance Proteome Discovery" addresses the most critical
challenge in biomarker discovery and progress: the identification
of low-abundance proteins. The book describes an original strategy
developed by the authorsthat permits the detection of protein
species typically found in very low abundance and that may yield
valuable clues to future discoveries. Known as combinatorial
peptide ligand libraries, these new methodologies are one of the
hottest topics related to the study of proteomics and have
applications in medical diagnostics, food quality, and plant
analysis. The book is written for university and industry
scientists starting proteomic studies of complex matrices (e.g.,
biological fluids, biopsies, recalcitrant plant tissues, foodstuff,
and beverage analysis), researchers doing wet chemistry, and
graduate-level students in the areas of analytical and
biochemistry, biology, and genetics.
Covers methodologies for enhancing the visibility of low-abundance
proteins which, until now, has been the biggest challenge in
biomarker progressIncludes detailed protocols that address
real-life needs in laboratory practiceAddresses all applications,
including human disease, food and beverage safety, and the
discovery of new proteins/peptides of importance in
nutraceuticsCompiles the research and analytic protocols of the two
scientists who are credited with the discovery of these landmark
methodologies, also known as combinatorial peptide ligand
libraries, for the identification of low-abundance proteins"
The book deals with the theory and practice of all electrophoretic
steps leading to proteome analysis, i.e. isoelectric focusing
(including immobilized pH gradients), sodium dodecyl sulphate
electrophoresis (SADS-PAGE) and finally two-dimensional maps. It is
a reasoned collection of all modern, relevant, up-to-date
methodologies leading to successful fractionation, analysis and
characterization of every polypeptide spot in 2-D map analysis. It
includes chapters on the most sophisticated mass spectrometry
developments and it helps the reader in navigating through the most
important databases in proteome analysis, including step by step
tours in selected sites. Yet, this book's unique strength and
feature is the fact that it combines not only practice (in common
with any other book on this topic) but also theory, by giving a
detailed treatment on the most advanced theoretical treatments of
steady-state techniques, such as isoelectric focusing and
immobilized pH gradients. A lot of this theory is newly developed
and presented to the public for the first time. Thus, this book
should satisfy not only the needs of every day practitioners, but
also the desires of the most advanced theoreticians in the field,
who will surely appreciate the novel theories presented here.
Also the methodological section contains several as yet
unpublished protocols, correcting some of the existing ones and
showing the pitfall and limitations of even well ingrained
protocols in proteome analysis, which are here critically
re-evaluated for the first time.
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