Abstract
Most proteomes of multi-cellular organisms are far more complex and have wider dynamic ranges of protein concentrations than the capacities of existing protein profiling methods. Hence, only modest portions of these proteomes, frequently less than 10% of the proteins, are detected and studied. The most effective solution to this disconnect between proteome complexity and protein profiling capacity is to simplify the biological samples of interest and focus on one or more subproteomes. A key factor in sample simplification strategies is to achieve reproducible isolation of an appropriate subproteome so that variations in preparations are not confused with biological changes. It is also important to be able to distinguish low-abundance components of the targeted subproteome from contaminants. While contamination can be greatly minimized, it can never be entirely eliminated. The specific subproteome that should be targeted depends heavily upon the biological questions being addressed. This session will highlight a number of current strategies for simplifying complex proteomes and their application to diverse biological and biomedical problems.