Bacterial infections and antibiotic resistance pose major challenges to human health that necessitates identification of novel antibiotic targets and new drug molecules.
In this study,the use of molecular dynamics(MD) simulations to reveal how mutations alter the structure and organization of enzyme active sites is presented.
DFT molecular dynamics(DFT-MD) calculations have been increasingly used as a means for generating several kind of spectra through the Fourier transform of specific autocorrelation functions[1].
Recently,molecular docking techniques have been widely used to predict the proteinli-gand binding-modes when the absent of the crystal complexes structures.
Based on the theoretical spectroscopic modeling,we calculate the isotope-edited equilibrium FTIR and 2DIR spectra of the two beta-hairpin peptides trpzip2 and trpzip4 using the nonlinear exciton propa
Hydroxynitrilelyases(HNLs)catalyze the cleavage of cyanohydrins into aldehyde(or ketone) and hydrocyanic acid(HCN).The release of HCN not only can protect plant system from herbivores and microbial at
The conformational dynamics of unsolvated polypeptides are investigated by ab inito molecular dynamics(AIMD) based on the generalized energy-based fragmentation(GEBF) approach.