Please use this identifier to cite or link to this item:
|Title:||Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition|
|Citation:||Sivakumar, N., Li, N., Tang, J.W., Patel, B.K.C., Swaminathan, K. (2006-05-15). Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition. FEBS Letters 580 (11) : 2646-2652. ScholarBank@NUS Repository. https://doi.org/10.1016/j.febslet.2006.04.017|
|Abstract:||Here we report the first crystal structure of a protein, AmyA, a secretory α-amylase isolated from Halothermothrix orenii, which is both halophilic and thermophilic. The crystal structure was determined at 1.6 Å resolution. AmyA lacks the conserved acidic surface, which is considered essential for protein stability at high salinity. Sedimentation velocity and CD experiments on AmyA reveal the formation of unique reversible poly-dispersed oligomers that show unusually high thermal stability. These studies provide valuable insight into the structural elements that contribute to the stability of AmyA at both physical and chemical extremes and their functional implications. © 2006.|
|Source Title:||FEBS Letters|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Sep 20, 2018
WEB OF SCIENCETM
checked on Sep 10, 2018
checked on Sep 21, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.