Proteins are molecular machines whose function depends on their ability to achieve
complex folds with precisely defined structural and dynamic properties. The rational design …

The goal of this article is to summarize what has been learned about the major forces
stabilizing proteins since the late 1980s when site-directed mutagenesis became possible …

Small molecule chaperones have been exploited as therapeutics for the hundreds of
diseases caused by protein misfolding. The most successful examples are the CFTR …

Proteins and their assemblies are fundamental for living cells to function. Their complex
three-dimensional architecture and its stability are attributed to the combined effect of …

The light-gated cation channel channelrhodopsin-2 (ChR2) has rapidly become an
important tool in neuroscience, and its use is being considered in therapeutic interventions …

Our goal was to gain a better understanding of the contribution of hydrophobic interactions
to protein stability. We measured the change in conformational stability, Δ (ΔG), for …

The emergent properties that arise from self-assembly and molecular recognition
phenomena are a direct consequence of non-covalent interactions. Gas-phase …

The features that stabilize the structures of membrane proteins remain poorly understood.
Polar interactions contribute modestly, and the hydrophobic effect contributes little to the …

An overview is presented of some of the major insights that have come from studies of the
structure, stability, and folding of T4 phage lysozyme. A major purpose of this review is to …

Background Bacteriorhodopsin (bR) is the simplest known light driven proton pump and has
been heavily studied using structural methods: eighty four X-ray diffraction, six electron …