background permanent antigenic variation of influenza viruses causes a major concern to develop an effective human influenza vaccine. conserved antigens are new vaccine candidates because it is not necessary to match the prepared vaccine with circulating strains. ion channel m2 protein is conserved among all influenza a viruses, allowing the virus to enter host cells. objectives to prepare an e...

Background: The chaperone activity of Mycobacterium tuberculosis Acr is an important function that helps to prevent misfolding of protein substrates inside the host, especially in conditions of hypoxia. Objectives: The aim of this study was to establish the correlation of structure and function of recombinant Acr proteins both before and after ge...

In lysosomal diseases, enzyme deficiency is caused by misfolding of mutant protein with abnormal steric structure that expressed gene mutation. Chaperone therapy a new molecular therapeutic approach primarily for diseases. The misfolded digested rapidly or aggregated to induce endoplasmic reticulum stress. As result, the catalytic activity lost. following sequence events results in chaperone ac...

We report on a study that combines advanced fluorescence methods with molecular dynamics simulations to cover timescales from nanoseconds milliseconds for large protein, the chaperone Hsp90.

Peroxiredoxin I (Prx I) plays an important role in cancer development and inflammation. It is a dual-functional protein which acts as both an antioxidant enzyme and a molecular chaperone. While there have been intensive studies on its peroxidase activity, Prx I's chaperone activity remains elusive, likely due to the lack of chaperone inhibitors. Here we report that natural product triptolide se...

We describe an efficient approach to model the binding interaction of the disordered effector protein to its cognate chaperone in the type III secretion system (T3SS). Starting from de novo models, we generated ensembles of unfolded conformations of the Yersinia effector YopE using REMD simulations and docked them to the chaperone SycE using a multistep protein docking strategy. The predicted Y...

Bacteria possess several molecular pathways to adapt changing environments and stress conditions. One of these involves a complex network chaperone proteins that together control proteostasis. In the aquatic bacterium Shewanella oneidensis, we have recently identified previously unknown co-chaperone DnaK/Hsp70 system, AtcJ, is essential for adaptation low temperatures. AtcJ encoded in atcJABC o...

Bacterial toxin-antitoxin (TA) systems, in which a labile antitoxin binds and inhibits the toxin, can promote adaptation and persistence by modulating bacterial growth in response to stress. Some atypical TA systems, known as tripartite toxin-antitoxin-chaperone (TAC) modules, include a molecular chaperone that facilitates folding and protects the antitoxin from degradation. Here we use a TAC m...