The field of drug discovery has witnessed infinite development over the last decade with the
demand for discovery of novel efficient lead compounds. Although the development of novel …

Proteins appear to fold by diverse pathways, but variations of a simple mechanism–
nucleation-condensation–describe the overall features of folding of most domains. In …

Proteobacteria constitute one of the most diverse and abundant groups of microbes on
Earth. In productive marine environments like deep-sea hydrothermal systems …

Molecular dynamics simulations of the protein chymotrypsin inhibitor 2 in 8 M urea at 60° C
were undertaken to investigate the molecular basis of chemical denaturation. The protein …

Heat-induced plant protein gels commonly require high protein concentration and
temperatures. However, hydrolysis of some plant proteins may promote their gelation under …

We can track the positions and movements of all the atoms in small proteins as they fold and
unfold by combining experimental studies with atomic-resolution molecular dynamics …

Proteins are very sensitive to their solvent environments. Urea is a common chemical
denaturant of proteins, yet some animals contain high concentrations of urea. These animals …

We compare the folding of representative members of a protein superfamily by experiment
and simulation to investigate common features in folding mechanisms. The homeodomain …

The effect of the electric field on the conformational properties of the protein 1BBL was
investigated by molecular dynamics simulations. Our simulation results clearly capture the …

All atom molecular dynamics simulations have become a standard method for mapping
equilibrium protein dynamics and non-equilibrium events like folding and unfolding. Here …