Transition metal catalysis is of utmost importance for the development of sustainable
processes in academia and industry. The activity and selectivity of metal complexes are …

Proteins are marginally stable, and the folding/unfolding equilibrium of proteins in aqueous
solution can easily be altered by the addition of small organic molecules known as …

Organisms use organic molecules called osmolytes to adapt to environmental conditions. In
vitro studies indicate that osmolytes thermally stabilize proteins, but mechanisms are …

Intrinsically disordered proteins (IDPs) adopt heterogeneous ensembles of conformations
under physiological conditions. Understanding the relationship between amino acid …

Many eukaryotic proteins are disordered under physiological conditions, and fold into
ordered structures only on binding to their cellular targets. Such intrinsically disordered …

Over the past few decades, there has been a tremendous increase in the utilization of
therapeutic peptides. Therapeutic peptides are usually administered via the parenteral …

The function, efficacy, and safety of protein biopharmaceuticals are tied to their three-
dimensional structure. The analysis and verification of this higher-order structure are critical …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

Protein stability often is studied in vitro through the use of urea and guanidinium chloride,
chemical cosolvents that disrupt protein native structure. Much controversy still surrounds …

Nature has selected osmolytes to protect intracellular macromolecules exposed to
denaturing conditions and stabilize proteins. Osmolytes are small naturally occurring …