Although protein folding is a simple outcome of the underlying thermodynamics, arriving at a
quantitative and predictive understanding of how proteins fold nevertheless poses huge …

The modern electron microscope, as a result of recent revolutionary developments and
many evolutionary ones, now yields a wealth of quantitative knowledge pertaining to …

The study of reaction mechanisms involves systematic investigations of the correlation
between structure, reactivity, and time. The challenge is to be able to observe the chemical …

In recent years the model on which the pharmaceutical industry is based has undergone
dramatic changes. Every year, more biological entities are being accepted by the FDA and …

Formation of α-helices is a fundamental process in protein folding and assembly. By
studying helix formation in molecular simulations of a series of alanine-based peptides, we …

The amyloid state of polypeptides is a stable, highly organized structural form consisting of
laterally associated β-sheet protofilaments that may be adopted as an alternative to the …

The relaxation of helical structures very close to equilibrium is observed via transient 2D IR
spectroscopy. An initial distribution of synthetically distorted helices having an unnatural …

For the past two decades, protein folding experiments have been speeding up from the
second or millisecond time scale to the microsecond time scale, and full-atom simulations …

An algorithm and software to refine parameters of empirical energy functions according to
condensed phase experimental measurements are discussed. The algorithm is based on …

As the simplest and most prevalent motif of protein folding, α-helix initiation is the starting
point of macromolecular complexity. In this work, helix initiation was directly measured via …