Please use this identifier to cite or link to this item:
http://dspace.uniten.edu.my/jspui/handle/123456789/9834
Title: | Application of the linear interaction energy method (LIE) to estimate the binding free energy values of Escherichia coli wild-type and mutant arginine repressor C-terminal domain (ArgRc)-L-arginine and ArgRc-L-citrulline protein-ligand complexes | Authors: | Asi, A.M. Rahman, N.A. Merican, A.F. |
Issue Date: | 2004 | Abstract: | Protein-ligand binding free energy values of wild-type and mutant C-terminal domain of Escherichia coli arginine repressor (ArgRc) protein systems bound to L-arginine or L-citrulline molecules were calculated using the linear interaction energy (LIE) method by molecular dynamics (MD) simulation. The binding behaviour predicted by the dissociation constant (Kd) calculations from the binding free energy values showed preferences for binding of L-arginine to the wild-type ArgRc but not to the mutant ArgRc(D128N). On the other hand, L-citrulline do not favour binding to wild-type ArgRc but prefer binding to mutant ArgRc(D128N). The dissociation constant for the wild-type ArgRc-L-arginine complex obtained in this study is in agreement with reported experimental results [J. Mol. Biol. 235 (1994) 221-230]. Our results also support the experimental data for the binding of L-citrulline to the mutant ArgRc(D128N) [J. Mol. Biol. 279 (1998) 753-760]. These showed that LIE method for protein-ligand binding free energy calculation could be applied to the wild-type and the mutant E. coli ArgRc-L-arginine and ArgRc-L-citrulline protein-ligand complexes and possibly to other transcriptional repressor-co-repressor systems as well. © 2003 Elsevier Inc. All rights reserved. | URI: | http://dspace.uniten.edu.my/jspui/handle/123456789/9834 |
Appears in Collections: | COE Scholarly Publication |
Show full item record
Google ScholarTM
Check
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.