Molecular chaperones impacts in growth, metabolism, pathogenicity and production of virulence factors in bacterial pathogen

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Abstract

Molecular chaperones are proteins that assist the valence folding or evolution and also the assembly or activity of different organic compound structures. In bacterial cell, the folding of expressed proteins is mainly occurred by preserved cytosolic chaperones, namely trigger factor. Many chaperones consider heat shock proteins, that is proteins expressed in response to elevated temperatures or alternative cellular stresses. Molecular chaperones are proteins responsible for varied processes in microbial cells, as well as helping the folding of new synthesized proteins, each throughout and when translation, helping in polypeptide secretion, and repairing proteins that are broken or misfolded by stress like a heat shock proteins. Molecular chaperones play a vital role in protein degradation, microbial adhesion activity and in responding to diseases joined to polypeptide (protein) aggregation.

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