Fluorescence arguably constitutes the most widely used experimental approach in the field
of protein folding. Hence, any review of the use of fluorescence to probe protein stability and …

Femtosecond visible and infrared analogues of multiple-pulse nuclear magnetic resonance
techniques provide novel snapshot probes into the structure and electronic and vibrational …

Accurate reproduction of the mechanism of peptide folding in solution and conformational
preferences as a function of amino acid sequence is possible with atomic level dynamics …

Obtaining the correct balance of secondary structure propensities is a central priority in
protein force-field development. Given that current force fields differ significantly in their α …

An implementation of classical molecular dynamics on parallel computers of increased
efficiency has enabled a simulation of protein folding with explicit representation of water for …

To meet the challenge of modeling the conformational dynamics of biological
macromolecules over long time scales, much recent effort has been devoted to constructing …

Protein chains coil into α-helices and β-sheet structures. Knowing the timescales and
mechanism of formation of these basic structural elements is essential for understanding …

The ensemble folding of two 21-residue α-helical peptides has been studied using all-atom
simulations under several variants of the AMBER potential in explicit solvent using a global …

We construct coarse master equations for peptide folding dynamics from atomistic molecular
dynamics simulations. A maximum-likelihood propagator-based method allows us to extract …

Proteins have dynamic structures that undergo chain motions on time scales spanning from
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …