▪ Abstract De novo protein design has recently emerged as an attractive approach for
studying the structure and function of proteins. This approach critically tests our …

Proteins are multifunctional in the sense that their specific amino acid sequence
simultaneously determines folding, function and degradation(Wetlaufer, 1980) …

Accurate reproduction of the mechanism of peptide folding in solution and conformational
preferences as a function of amino acid sequence is possible with atomic level dynamics …

The kinetics of formation of protein structural motifs (eg, α-helices and β-hairpins) can
provide information about the early events in protein folding. A recent study has used …

The fine‐tuning of the protecting groups and the glycosidation conditions were the key to the
successful coupling of the carbohydrate units and vancomycin aglycon in the last steps of …

We used UV resonance Raman spectroscopy to characterize the equilibrium conformation
and the kinetics of thermal denaturation of a 21 amino acid, mainly alanine, α-helical peptide …

▪ Abstract During protein folding, many of the events leading to secondary and tertiary
structure occur in milliseconds or faster. Modern nuclear magnetic resonance and laser …

NMR studies of the folding and conformational properties of a β-hairpin peptide, several
peptide fragments of the hairpin, and sequence-modified analogues, have enabled the …

For many proteins, compact conformations are known to accumulate in advance of the rate-
limiting step in folding. To understand the nature and significance of these early …

Considerable insights into the mechanisms and timescales of protein folding have been
obtained from detailed studies of minimal off-lattice models. These models are coarse …