Understanding the molecular mechanisms of enzyme catalysis and allosteric regulation has
been a primary goal of biochemistry for many years. The dynamics of these processes …

In this overview, we discuss theoretical and experimental aspects of nonlinear two-
dimensional infrared (2D-IR) spectroscopy. With this technique both peptide conformation …

We study atomic models of the thermodynamics of the structural transition of peptides that
form α-helices. The effect of sequence variation on α-helix formation for alanine-rich …

The helix-coil transition kinetics of an α-helical peptide were investigated by time-resolved
infrared spectroscopy coupled with laser-induced temperature-jump initiation method …

Femtosecond time-resolved spectroscopy on model peptides with built-in light switches
combined with computer simulation of light-triggered motions offers an attractive integrated …

Several molecular dynamics simulations were performed on three proteins—bovine apo‐
calbindin D9K, human interleukin‐4 R88Q mutant, and domain IIA of bacillus subtilis …

There have been recent advances in initiating and perturbing chemical reactions on very
fast timescales, as short as picoseconds, thus making it feasible to study a vast range of …

Structural parameters for standard peptide helices (α, 310, 31 left‐handed) were fully ab
initio optimized for Ac–(l‐Ala) 9–NHMe and for Ac–(l‐Pro) 9–NHMe (poly‐l‐proline—PLP I …

▪ Abstract An explosion of in vitro experimental data on the folding of proteins has revealed
many examples of folding in the millisecond or faster timescale, often occurring in the …

Publisher Summary Unfolded proteins and unstructured peptides form vital thermodynamic
states critical to the overall protein folding problem. They represent one of a possible set of …