![]() ![]() However, calculated correlation times and changes in amide protection from hydrogen/deuterium exchange experiments provide evidence for a loosening of the tertiary and quaternary structures of HdeA in particular, the data indicate that the dimer structure becomes progressively weakened as the pH decreases. Measurements of R 2/ R 1 ratios from relaxation experiments confirm that the protein maintains its dimer structure between pH 6.0 and 3.0. NMR spectroscopy was used to measure pK a values of Asp and Glu residues and monitor chemical shift changes. The goal for this study, therefore, was to investigate, at the atomic level, the structural impact of this charge neutralization on HdeA during the transition from near-neutral conditions to pH 3.0, in preparation for unfolding and activation of its chaperone capabilities. ![]() It has been argued that one of the major driving forces for HdeA activation is the protonation of aspartate and glutamate side chains. ![]() After the protein becomes activated at low pH, it can bind to other periplasmic proteins, protecting them from aggregation when the bacteria travel through the stomach on their way to colonize the intestines. HdeA is a periplasmic chaperone found in several gram-negative pathogenic bacteria that are linked to millions of cases of dysentery per year worldwide.
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |