Protein–protein interactions (PPIs) are involved at all levels of cellular organization, thus
making the development of PPI inhibitors extremely valuable. The identification of selective …

The construction of complex protein folds relies on the precise conversion of a linear
polypeptide chain into a compact 3-dimensional structure. The interplay of forces that link …

Nature relies on large molecules to carry out sophisticated chemical operations, such as
catalysis, tight and specific binding, directed flow of electrons, or controlled crystallization of …

The construction of bioactive peptides using β-amino acid-containing sequence patterns is a
very promising strategy to obtain analogues that exhibit properties of high interest for …

To establish a framework for extrapolating the helix-forming properties of peptides from
TFE/H2O mixtures (TFE= 2, 2, 2-trifluoroethanol) back to water, the thermal unfolding curves …

Protein chains coil into α-helices and β-sheet structures. Knowing the timescales and
mechanism of formation of these basic structural elements is essential for understanding …

The information about the conformational behavior of monomeric helical peptides in
solution, as well as the α-helix stability in proteins, has been previously utilized to derive a …

▪ 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 …

The remarkable complexity of globular protein structures was first revealed about half a
century ago, when the crystal structure of myoglobin was determined at 2.4 Å. 1 In the …

The folding reactions of some small proteins show clear evidence of a hierarchic process,
whereas others, lacking detectable intermediates, do not. Nevertheless, we argue that both …