Abstract
Our laboratory has previously used a limited proteolysis mass-spectrometry (LiP-MS) approach to show that a third of the soluble E. coli proteome is unable to efficiently refold to their native structures on physiological timescales following denaturation. In this method, we take advantage of a permissive protease that preferentially cleaves at more flexible regions to examine structural differences between native and refolded lysates. Here, we seek to apply this technique to the proteomes of different mesophilic fungi and bacteria across various phylogenetic clades.
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