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...

bacterial and viral triggers are suspected agents in the initial etiology of autoimmune diseases. there are some studies on the etiology of autoimmune disorders which have focused on streptococcal infection and a possible relation with microbial heat shock proteins (hsp) which show significant homology with human heat shock proteins. in addition, some serotypes of streptococci cross-react with ...

Guiding of relativistically intense (>10(18) W/cm2) laser pulses over more than 10 diffraction lengths has been demonstrated using plasma channels formed by hydrodynamic shock. Pulses up to twice the self-guiding threshold power were guided without aberration by tuning the guide profile. Transmitted spectra and mode images showed the pulse remained in the channel over the entire length. Experim...

The respiration of Escherichia coli is severely inhibited, during hyperosmotic stress period, as a consequence of plasmolysis; deplasmolysis allows the cell to recover respiration. A mutant lacking all K+ transport systems can neither deplasmolyze nor recover respiration unless betaine is present in the medium. Betaine, in these conditions, increases both cytoplasmic volume and respiration; thi...

Small heat shock proteins (sHSPs) are dynamic oligomeric proteins that bind unfolding proteins and protect them from irreversible aggregation. This binding results in the formation of sHSP-substrate complexes from which substrate can later be refolded. Interactions between sHSP and substrate in sHSP-substrate complexes and the mechanism by which substrate is transferred to ATP-dependent chapero...

Heat-shock proteins DnaK, DnaJ, and GrpE (KJE) from Escherichia coli constitute a three-component chaperone system that prevents aggregation of denatured proteins and assists the refolding of proteins in an ATP-dependent manner. We found that the rate of KJE-mediated refolding of heat- and chemically denatured proteins is decreased at high temperatures. The efficiency and reversibility of prote...

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