Themis Lazaridis

TL;DR: An overview of the CHARMM program as it exists today is provided with an emphasis on developments since the publication of the original CHARMM article in 1983.

TL;DR: Results reported elsewhere show that EEF1 clearly distinguishes correctly from incorrectly folded proteins, both in static energy evaluations and in molecular dynamics simulations and that unfolding pathways obtained by high‐temperature Molecular dynamics simulations agree with those obtained by explicit water simulations.

TL;DR: A synthesis of the "new" and the classical view of protein folding with a preferred pathway on a funnel-like average energy surface is suggested.

TL;DR: The benefits, challenges, and opportunities of using antimicrobial peptides against multidrug-resistant pathogens are identified, advances in the deployment of novel promising antimacterial peptides are highlighted, and the needs and priorities in designing focused development strategies taking into account the most advanced tools available are underlined.

TL;DR: Molecular mechanics force fields, particularly when augmented by implicit solvation models, provide physical effective energy functions that are beginning to play a role in protein structure prediction, fold recognition, homology modeling and design.