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 …

Proteins appear to fold by diverse pathways, but variations of a simple mechanism–
nucleation-condensation–describe the overall features of folding of most domains. In …

α-Synuclein (αS) is a presynaptic terminal protein that is believed to play an important role in
the pathogenesis of Parkinson's disease (PD). We have used NMR spectroscopy to …

Non-native states of proteins are of increasing interest because of their relevance to issues
such as protein folding, translocation and stability. A framework for interpreting the wealth of …

Inclusion bodies (IBs) often emerge upon overexpression of recombinant proteins in E. coli.
From IBs, refolding is necessary to generate the native protein that can be further purified to …

Publisher Summary Protein folding is a process by which a polypeptide chain acquires its
native structure from an unfolded state through a transition state. Recent studies of the …

Studies of proteins unfolded in acid or chemical denaturant can help in unraveling events
during the earliest phases of protein folding. In order for meaningful comparisons to be …

It is generally assumed that folding intermediates contain partially formed native-like
secondary structures. However, if we consider the fact that the conformational stability of the …

Publisher Summary Nuclear magnetic resonance (NMR) is unique in being able to provide
detailed insights into the conformation of unfolded and partly folded proteins. This chapter …

A database of hydrogen-deuterium exchange results has been compiled for proteins for
which there are published rates of out-exchange in the native state, protection against …