We use a combination of experiments, computer simulations and simple model calculations
to characterize, first, the folding transition state ensemble of the src SH3 domain, and …

The folding and unfolding kinetics of the B-domain of staphylococcal protein A, a small three-
helix bundle protein, were probed by NMR. The lineshape of a single histidine resonance …

Over the past 25 years, enormous breakthroughs have been made in understanding protein
folding mechanisms. We have now reached an exciting stage, with consensuses beginning …

The 62 residue IgG binding domain of protein L consists of a central α-helix packed on a four-
stranded β-sheet formed by N and C-terminal β-hairpins. The overall topology of the protein …

Protein Folding Kinetics-Biophysical Methods (2nd Edition) gives a deep insight into the
principles and concepts of the kinetic and structural resolution of fast chemical and …

The development of the EGAD program and energy function for protein design is described.
In contrast to most protein design methods, which require several empirical parameters or …

High hydrostatic pressures (1–2 kbar), combined with low, nondenaturing concentrations of
guanidine hydrochloride (GdmHCl) foster disaggregation and refolding of denatured and …

▪ Abstract We outline recent developments in biological single-molecule fluorescence
detection with particular emphasis on observations by ratiometric fluorescence resonance …

Reduced computer modeling of proteins now has a history of about 30 years. In spite of the
enormous increase in computing abilities, reduced models are still very important tools for …

Amino acid networks (AANs) are undirected networks consisting of amino acid residues and
their interactions in three-dimensional protein structures. The analysis of AANs provides …