Protein folding and aggregation in bacteria.

摘要: Proteins might experience many conformational changes and interactions during their lifetimes, from synthesis at ribosomes to controlled degradation. Because, in most cases, only folded proteins are functional, protein folding bacteria is tightly genetically, transcriptionally, the sequence level. In addition, important cellular machinery assists of polypeptides avoid misfolding ensure attainment functional structures. When these redundant protective strategies overcome, misfolded recruited into insoluble inclusion bodies. The embedded intracellular deposits display different conformations including β-sheet-rich latter assemblies similar amyloid fibrils characteristic several human neurodegenerative diseases. Interestingly, exploit same structural principles for properties such as adhesion or cytotoxicity. Overall, this review illustrates how prokaryotic organisms provide bedrock on which understand complexity aggregation cell.