例如:"lncRNA", "apoptosis", "WRKY"

Denaturant-induced unfolding of the acetyl-esterase from Escherichia coli.

Biochemistry. 2004 Nov 23;43(46):14637-43. doi:10.1021/bi048344f
Pompea Del Vecchio 1 , Giuseppe Graziano , Vincenzo Granata , Tiziana Farias , Guido Barone , Luigi Mandrich , Mosè Rossi , Giuseppe Manco
Pompea Del Vecchio 1 , Giuseppe Graziano , Vincenzo Granata , Tiziana Farias , Guido Barone , Luigi Mandrich , Mosè Rossi , Giuseppe Manco
+ et al

[No authors listed]

Author information
  • 1 Department of Chemistry, University of Naples Federico II, Italy. delvecchio@chemistry.unina.it

摘要


The stability of acetyl-esterase, Aes, from Escherichia coli against the denaturing action of urea and guanidine hydrochloride, GuHCl, has been investigated by means of circular dichroism and fluorescence measurements. The urea-induced unfolding curves show a single inflection point at 6.2 M urea, whereas the GuHCl-induced curves show two inflection points at 1.4 and 3.1 M GuHCl. The unfolding process is reversible with both urea and GuHCl. These results, together with similar experimental data on the mutant form V20D-Aes, suggest the presence of two domains in the Aes structure, which unfold more or less independently depending on the denaturant used. This is also supported by a 3D model obtained by homology modeling using the structure of brefeldine as a template. The effect of NaCl on the urea-induced unfolding curves of the enzyme has also been investigated.

基因