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- W2364253181 abstract "Small heat shock proteins,a family of heat shock proteins ubiquitously present both in prokaryotes and eukaryotes,form specific oligomeric structures of 200—800 kD,with the monomer size between 12 and 43 kD.The small heat shock protein from %Mycobacterium tuberculosis%,Hsp16^3 was previously shown to form a specific nonameric structure,existing as a trimer of trimers.The subunit interaction in the reassembly process of this oligomeric protein was investigated using wild type Hsp16^3 and the L122A mutant protein,non|denaturing polyacrylamide gel electrophoresis and urea gradient polyacrylamide gel electrophoresis.The results show that Leu122 plays an important role in the subunit interaction in the assembly process of Hsp16^3.There are no hybrid intermediates formed during the %in vitro% co|assembly process of wild type Hsp16^3 and the L122A mutant,which strongly suggests that only identical subunites of Hsp16^3 can specifically recognize each other and form oligomer." @default.
- W2364253181 created "2016-06-24" @default.
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- W2364253181 date "2002-01-01" @default.
- W2364253181 modified "2023-09-26" @default.
- W2364253181 title "The Effect of Leu122 on the Subunit Interaction in the Reassembly of Hsp16.3 in vitro" @default.
- W2364253181 hasPublicationYear "2002" @default.
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