Recent experimental developments are changing the ways we interpret experimental data in
protein folding, leading to a closer connection with theory and an improved understanding of …

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

For an isolated resonance of an isolated chromophore in a condensed phase, the
absorption line shape is often more sharply peaked than the distribution of transition …

Using time-resolved IR spectroscopy, we monitored the kinetics of folding and unfolding
processes of a photoswitchable 16-residue alanine-based α-helical peptide on a timescale …

We have developed a Fourier transform two-dimensional infrared (2D IR) spectrometer to
probe chemical reactions and biophysical processes triggered by a nanosecond …

Short peptides that fold into β‐hairpins are ideal model systems for investigating the
mechanism of protein folding because their folding process shows dynamics typical of …

The FF domain from the human protein HYPA/FBP11 folds via a low-energy on-pathway
intermediate (I). Elucidation of the structure of such folding intermediates and denatured …

The coupling of a coarse-grained (CG) protein model with the CG water model developed by
Marrink et al.(J. Phys. Chem. B 2004, 108, 750) is presented. The model was used in the …

The laws of thermodynamics provide a clear concept of the temperature for an equilibrium
system in the continuum limit. Meanwhile, the equipartition theorem allows one to make a …

The α-helix is a ubiquitous structural element in proteins, and a number of studies have
addressed the mechanism of helix formation and melting in simple peptides. However …