Preparation of biological macromolecules in the pure state requires that cells be disrupted,
releasing and mixing the contents. Only the most stable and highly structured molecules can …

Protein aggregation has now become recognised as an important and generic aspect of
protein energy landscapes. Since the discovery that numerous human diseases are caused …

Intrinsically disordered proteins (IDPs), which lack folded structure and are disordered under
nondenaturing conditions, have been shown to perform important functions in a large …

The roles of unfolded states of proteins in normal folding and in diseases involving
aggregation, as well as the prevalence and regulatory functions of intrinsically disordered …

Vibrational spectroscopy provides a direct route to the physicochemical characterization of
molecules. While both IR and Raman spectroscopy have been used for decades to provide …

Obtaining detailed structural models of disordered states of proteins under nondenaturing
conditions is important for a better understanding of both functional intrinsically disordered …

Disordered states of proteins include the biologically functional intrinsically disordered
proteins and the unfolded states of normally folded proteins. In recent years, ensemble …

Protection factors obtained from equilibrium hydrogen exchange experiments are an
important source of structural information on both native and nonnative states of proteins …

Due to their dynamic ensemble nature and a deficiency of experimental restraints,
disordered states of proteins are difficult to characterize structurally. Here, we have …

The cosolvent effect arises from the interaction of cosolute molecules with a protein and
alters the equilibrium between native and unfolded states. Denaturants shift the equilibrium …