Thermal denaturing of mutant lysozyme with both the OPLSAA and the CHARMM force fields.

@article{Eleftheriou2006ThermalDO,
  title={Thermal denaturing of mutant lysozyme with both the OPLSAA and the CHARMM force fields.},
  author={Maria Eleftheriou and Robert S. Germain and Ajay K. Royyuru and Ruhong Zhou},
  journal={Journal of the American Chemical Society},
  year={2006},
  volume={128 41},
  pages={
          13388-95
        }
}
Biomolecular simulations enabled by massively parallel supercomputers such as BlueGene/L promise to bridge the gap between the currently accessible simulation time scale and the experimental time scale for many important protein folding processes. In this study, molecular dynamics simulations were carried out for both the wild-type and the mutant hen lysozyme (TRP62GLY) to study the single mutation effect on lysozyme stability and misfolding. Our thermal denaturing simulations at 400-500 K with… CONTINUE READING
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