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Bradyrhizobium
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Oligomerization into multimeric complexes is a prerequisite for the chaperone function of almost all a-crystallin type heat shock proteins (a-Hsp), but the molecular details of complex assembly are poorly understood. The a-Hsp proteins from Bradyrhizobium japonicum are suitable bacterial models for structure-function studies of these ubiquitous stress proteins. They fall into two distinct classes, A and B, display chaperone activity in vitro and form oligomers of 24 subunits.
9p
research12
01-06-2013
54
6
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The effect of pH and temperature on structure, stability, activity and enantioselectivity of haloalkane dehalogenase DbjA from Bradyrhizobium japonicum USDA110 was investigated in this study. Conformational changes have been assessed by circular dichroism spectroscopy, functional changes by kinetic analysis, while quaternary structure was studied by gel filtration chromatography.
11p
cosis54
05-01-2013
57
4
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