After more than one year of implementation under Decision No. 19 / QD-KHCNTT dated January 24^th, 2017 about promulgating the Internal Spending Rules of the Institute for Computational Science and Technology, based on Clause 1, Article 14 of the Rules, which stipulates support for International and domestic publication. There are some publications of the official researchers at the ICST supported by the funds. Recently, there is a new publication of researchers Hung Nguyen, Tri Pham and Tuyn Phan. Here is an introduction to the publication of the researchers.
 
On July 13^th, 2017, researcher of Open Lab at ICST (Hung Nguyen), and his colleagues, Tri Pham, Tuyn Phan, have just published a research named “Steered Molecular Dynamics for Investigating the Interactions Between Insulin Receptor Tyrosine Kinase (IRK) and Variants of Protein Tyrosine Phosphatase 1B (PTP1B)” on “Applied Biochemistry and Biotechnology”


 
The aim of this study is to use steered molecular dynamics to investigate the dissociation process between IRK and PTP1Bs for wild type and five mutants (consisting of p.D181E, p.D181A, p.Q262A, p.D181A-Y46F, and p.D181A-Q262A). The gained results are observed not only the unbinding mechanism of IRK-PTP1B complexes came from pulling force profile, number of hydrogen bonds, and interaction energy between IRK and PTP1Bs but also described PTP1B’s point mutations could variably change its binding affinity towards IRK. Additionally, the binding free energy calculated by Molecular Mechanics/PoissonBoltzmann Surface Area (MM-PBSA) is also revealed that electrostatic energy and polar solvation energy mainly made up the binding free energy of PTP1B-IRK complexes.


Read full article here.

Editor: Kim Loan