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

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 …

We show how accurate kinetic information, such as the rates of protein folding and
unfolding, can be extracted from replica-exchange molecular dynamics (REMD) simulations …

Helix formation is an elementary process in protein folding, influencing both the rate and
mechanism of the global folding reaction. Yet, because helix formation is less cooperative …

It is well-known that end caps and the peptide length can dramatically influence the
thermodynamics of the helix− coil transition. However, their roles in determining the kinetics …

The energetics and hydrogen bonding profiles of the helix-to-coil transition were found to be
an additive property and to increase linearly with chain length, respectively, in alanine-rich α …

α-helices being the most common secondary structures found ubiquitously in proteins, have
been studied extensively for elucidating its folding dynamics and mechanism. In addition …

A microscopic spin model is proposed for the phenomenological Zimm-Bragg model for the
helix-coil transition in biopolymers. This model is shown to provide the same thermophysical …

The nucleation event in α-helix formation is a fundamental process in protein folding.
However, determining how quickly it takes place based on measurements of the relaxation …

The thermally-induced helix–coil transition in polyamino acids is a good model for
determining the helix-forming propensities of amino acids but not for the two-state …