Characterization of the Escherichia coli YedU protein as a molecular chaperone
We have cloned, purified to homogeneity, and characterized as a molecular chaperone the Escherichia coli YedU protein. The purified protein shows a single band at 31 kDa on SDS–polyacrylamide gels and forms dimers in solution. Like other chaperones, YedU interacts with unfolded and denatured protein...
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| Format: | article |
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2003
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| Online Access: | http://hdl.handle.net/10725/4161 http://dx.doi.org/10.1016/S0006-291X(02)03053-X http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php http://www.sciencedirect.com/science/article/pii/S0006291X0203053X |
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