Large-scale analysis of thermostable, mammalian proteins provides insights into the intrinsically disordered proteome.

摘要: Intrinsically disordered proteins are predicted to be highly abundant and play broad biological roles in eukaryotic cells. In particular, by virtue of their structural malleability propensity interact with multiple binding partners, thought specialized for signaling regulation. However, these concepts based on silico analyses translated whole genome sequences, not large-scale expressed living Therefore, whether broadly apply is currently unknown. Previous studies have shown that heat-treatment cell extracts lead partial enrichment soluble, proteins. On the basis this observation, we sought address current dearth knowledge about expressed, performing a proteomics study thermostable isolated from mouse fibroblast With use novel multidimensional chromatography methods mass spectromet...