Atomistic simulations of protein folding have the potential to be a great complement to
experimental studies, but have been severely limited by the time scales accessible with …

Most small, single‐domain proteins fold with the uncomplicated, single‐exponential kinetics
expected for diffusion on a smooth energy landscape. Despite this energetic smoothness …

Guided by the recent success of empirical model predicting the folding rates of small two‐
state folding proteins from the relative contact order (CO) of their native structures, by a …

Combining experimental and simulation data to describe all of the structures and the
pathways involved in folding a protein is problematical. Transition states can be mapped …

We have used laser temperature-jump to investigate the kinetics and mechanism of folding
the 35 residue subdomain of the villin headpiece. The relaxation kinetics are biphasic with a …

The conformational equilibrium between 310‐and α‐helical structure has been studied via
high‐resolution NMR spectroscopy by Millhauser and coworkers using the MW peptide Ac …

Here, we describe the folding/unfolding kinetics of α3D, a small designed three-helix bundle.
Both IR temperature jump and ultrafast fluorescence mixing methods reveal a single …

Recent advances have significantly increased the time and spectroscopic resolution of
protein folding experiments. We can now study the timescale and nature of polypeptide …

The thermal stability and folding kinetics of a 15-residue β-hairpin (SESYINPDGTWTVTE)
have been studied by using infrared (IR) spectroscopy coupled with laser-induced …

Twelve mutations were constructed to improve the thermostability of glucoamylase from
Aspergillus awamori based on the results of molecular dynamics simulations. The thermal …