Publisher Summary This chapter deals with the structure of the molten globules of various
globular proteins revealed by the recent experimental studies. Recent advances in …

Hydrogen/deuterium (H/D) exchange combined with two-dimensional (2D) NMR
spectroscopy has been widely used for studying the structure, stability, and dynamics of …

Prions, the causative agents of Creutzfeldt-Jacob Disease (CJD) in humans and bovine
spongiform encephalopathy (BSE) and scrapie in animals, are principally composed of PrP …

Do stable intermediates form very early in the protein folding process? New results and a
quantity of literature that bear on this issue are examined here. Results available provide …

Submillisecond burst phase signals measured in kinetic protein folding experiments have
been widely interpreted in terms of the fast formation of productive folding intermediates …

The partly folded state of apomyoglobin at pH 4 represents an excellent model for an
obligatory kinetic folding intermediate. The structure and dynamics of this intermediate state …

It is demonstrated that the identity of residues accessing excited conformational states that
are of low free energy relative to the ground state in proteins can be obtained from amide …

The denaturant-dependence of the major, observable relaxation rates for folding (kobs) of
ribonuclease HI from Escherichia coli (RNase H) and phage T4 lysozyme (T4L) reveal that …

Experiments were designed to explore the tolerance of protein structure and folding to very
large insertions of folded protein within a structural domain. Dihydrofolate reductase and β …

Distinguishing between competing pathways of folding of a protein, on the basis of how they
differ in their progress of structure acquisition, remains an important challenge in protein …