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pro vyhledávání: '"Xiuguang FENG"'
Publikováno v:
Journal of Molecular Biology. 326:1013-1023
Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis proposed to form specific trimer-of-trimers structures, acts as a molecular chaperone in vitro. The assembly and re-assembly mechanisms of this oligomeric protein were studied and co
Publikováno v:
Biochemical and Biophysical Research Communications. 284:942-947
The in vitro chaperone-like activity of Mycobacterium tuberculosis small heat shock protein Hsp16.3 was found to be dramatically enhanced to the same extent after preheat treatment at or over 60 degrees C. Structural analysis using gel filtration, na
Conditions are reported under which the reassembled intermediates of the heat-shock protein Hsp16.3 after being denatured in 8M urea were detected by mainly using urea-gradient PAGE (with modifications) and urea-denaturing pore-gradient PAGE. Hsp16.3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95188453d95dc90317ed40147fa0e9fa
https://europepmc.org/articles/PMC1222482/
https://europepmc.org/articles/PMC1222482/