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The term “kinetic stability” (KS) is sometimes used to describe proteins that are conformationally trapped by the presence of an unusually high-energy unfolding barrier that considerably decreases their unfolding rate under various conditions. This barrier allows kinetically stable proteins (KSPs) to maintain their fold and activity over longer periods, even in inhospitable environments. KS is likely to play important biological roles, such as the regulation of protein turnover, protection from proteolytic degradation, and blocking access to aggregation-prone conformations. However, the chemical-physical basis and the diversity of biological-pathological roles of protein KS remain poorly understood, in part because for many years the study of KS was limited to individual pure proteins, and involved spectroscopic instrumentation that was not available to most researchers. In this chapter, we will review the discovery of a correlation between a protein’s KS and its resistance to the detergent sodium dodecyl sulfate (SDS), and the subsequent development of a diagonal two-dimensional (D2D) SDS-PAGE assay and capillary electrophoresis approaches to identify the proteome of KSPs in any cell or organism.

Proteomics Analysis of Kinetically Stable Proteins