NMR is very well suited to the study of especially weak protein− protein interactions, as no
crystallization is required. The available NMR methods to this end are reviewed and …

▪ Abstract Beginning with simplified lattice and continuum “minimalist” models and
progressing to detailed atomic models, simulation studies have augmented and directed …

How did specific useful protein sequences arise from simpler molecules at the origin of life?
This seemingly needle-in-a-haystack problem has remarkably close resemblance to the old …

A central tenet of biology is that globular proteins have a unique 3D structure under
physiological conditions. Recent work has challenged this notion by demonstrating that …

▪ Abstract Mass spectrometry has provided a powerful method for monitoring hydrogen
exchange of protein backbone amides with deuterium from solvent. In comparison to …

We relate the unfolding of a protein to its loss of structural stability or rigidity. Rigidity and
flexibility are well defined concepts in mathematics and physics, with a body of theorems …

Despite numerous efforts, the lack of detailed structural information on amyloid fibrils has
hindered clarification of the mechanism of their formation. Here, we describe a novel …

We present a framework for studying protein folding pathways and potential landscapes
which is based on techniques recently developed in the robotics motion planning …

Fold-switching proteins respond to cellular stimuli by remodeling their secondary structures
and changing their functions. Whereas several previous reviews have focused on various …

Analysis of the kinetics of hydrogen exchange in biological macromolecules is a powerful
method for studying both their structural and dynamic properties. This arises from our …