Antimicrobial peptides (AMPs) take part in the immune system by mounting a first line of
defense against pathogens. Recurrent structural and functional aspects are observed …

For 35 years, the prevailing view has been that the hydrophobic effect is the dominant force
in protein folding. The importance of hydrogen bonding was always clear, but whether it …

Over the past decade, major progress in supramolecular polymerization has had a
substantial effect on the design of functional soft materials. However, despite recent …

The average globular protein contains 30% α-helix, the most common type of secondary
structure. Some amino acids occur more frequently in α-helices than others; this tendency is …

Obtaining the correct balance of secondary structure propensities is a central priority in
protein force-field development. Given that current force fields differ significantly in their α …

A Gaussian solvent‐exclusion model for the solvation free energy is developed. It is based
on theoretical considerations and parametrized with experimental data. When combined …

The first fully automated design and experimental validation of a novel sequence for an
entire protein is described. A computational design algorithm based on physical chemical …

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 …

Using an empirical analysis of experimental data we have estimated a set of energy
contributions which accounts for the stability of isolated α-helices. With this database and an …

Publisher Summary This chapter summarizes the experimental information on protein
energetics. This field is developing fast and the concept of the energetics of protein structure …