Although phenomenlogical models that account for cooperativity in allosteric systems date
back to the early and mid‐60's (eg, the KNF and MWC models), there is resurgent interest in …

The atomic force microscope (AFM) has a unique capability of allowing the high-resolution
imaging of biological samples on substratum surfaces in physiological solutions. Recent …

Cryoelectron microscopy of biological molecules is among the hottest growth areas in
biophysics and structural biology at present, and Frank is arguably the most distinguished …

Chaperonins are large ring assemblies that assist protein folding to the native state by
binding nonnative proteins in their central cavities and then, upon binding ATP, release the …

Chaperonins are large barrel-shaped complexes that mediate ATP-dependent protein
folding,–. The bacterial chaperonin GroEL forms juxtaposed rings that bind unfolded protein …

The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of
Escherichia coli. Here we show that GroEL interacts strongly with a well-defined set of …

▪ Abstract Molecular chaperones are required to assist folding of a subset of proteins in
Escherichia coli. We describe a conceptual framework for understanding how the GroEL …

Conventional atomic force microscopes (AFMs) take at least 30–60 s to capture an image,
while dynamic biomolecular processes occur on a millisecond timescale or less. To narrow …

A novel contour-based matching criterion is presented for the quantitative docking of high-
resolution structures of components into low-resolution maps of macromolecular complexes …

We have used a prototype small cantilever atomic force microscope to observe, in real time,
the interactions between individual protein molecules. In particular, we have observed …