Abstract
Some proteins in nature are kinetically stable, as indicated by their very slow unfolding and resistance to degradation, even under relatively harsh conditions. Aside from preventing protein aggregation or their premature degradation, the extent of biological roles related to kinetic stability remain poorly understood. Proteins with high kinetic stability are resistant to SDS, and therefore they may be identified at a proteomics level via diagonal two-dimensional (D2D) SDS-PAGE. We have applied D2D SDS-PAGE and related methods to identify kinetically stable proteins in diverse systems, including bacteria, legumes/nuts, and human plasma. The results of these studies have provided new insight about the significance of protein kinetic stability in organismal adaptation and longevity. In addition, the analysis of a growing list of SDS-resistant proteins generated from these studies is enhancing our understanding of the structural basis of protein kinetic stability.
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