The use of small-angle X-ray solution scattering (SAXS) as an analytical chemical tool for
structural molecular biology is a mature field dating back to the work of Glatter and Kratky in …

Despite its theoretical and practical importance, protein folding remains among the most
fundamental unsolved problems in the life sciences. The challenge of predicting folded …

Structural analysis of flexible macromolecular systems such as intrinsically disordered or
multidomain proteins with flexible linkers is a difficult task as high-resolution techniques are …

Spectroscopic studies have identified a number of proteins that appear to retain significant
residual structure under even strongly denaturing conditions. Intrinsic viscosity …

We study the effect of pH and temperature on fibril formation from hen egg white lysozyme.
Fibril formation is promoted by low pH and temperatures close to the midpoint temperature …

The Gaussian-distributed random coil has been the dominant model for denatured proteins
since the 1950s, and it has long been interpreted to mean that proteins are featureless …

The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA. This talk will provide
an overview of new approaches to study and manipulate signaling in living cells and …

Proteins are adjustable units from which biomaterials with designed properties can be
developed. However, non-native folded states with controlled topologies are hardly …

Conditions including heating mode, time, temperature, pH, moisture and protein
concentration, shear, and the presence of alcohols, chaotropic/reducing agents, enzymes …

Publisher Summary This chapter reviews recent small-angle X-ray and neutron scattering
(SAXS and SANS) studies of putatively “fully” unfolded states formed at equilibrium. It …