Title: High temperature unfolding of Bacillus anthracis amidase-03 by molecular dynamics simulations
Authors: Sharma, Ravi Datta ×
Lynn, Andrew M
Sharma, Pradeep Kumar
Kanwal, Rajnee
Jawaid, Safdar #
Issue Date: 2009
Publisher: Biomedical Informatics Pub. Group
Series Title: Bioinformation vol:3 issue:10 pages:430-4
Abstract: The stability of amidase-03 structure (a cell wall hydrolase protein) from Bacillus anthracis was studied using classical molecular dynamics (MD) simulation. This protein (GenBank accession number: NP_844822) contains an amidase-03 domain which is known to exhibit the catalytic activity of N-acetylmuramoyl-L-alanine amidase (digesting MurNAc-Lalanine linkage of bacterial cell wall). The amidase-03 enzyme has stability at high temperature due to the core formed by the combination of several secondary structure elements made of beta-sheets. We used root-mean-square-displacement (RMSD) of the simulated structure from its initial state to demonstrate the unfolding of the enzyme using its secondary structural elements. Results show that amidase-03 unfolds in transition state ensemble (TSE). The data suggests that alpha-helices unfold before beta-sheets from the core during simulation.
ISSN: 0973-2063
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Non-KU Leuven Association publications
× corresponding author
# (joint) last author

Files in This Item:
File Description Status SizeFormat
97320630003430.pdfMolecularSimulationAmidas03 Published 223KbAdobe PDFView/Open Request a copy

These files are only available to some KU Leuven Association staff members


All items in Lirias are protected by copyright, with all rights reserved.