Natural metalloproteins perform many functions—ranging from sensing to electron transfer
and catalysis—in which the position and property of each ligand and metal are dictated by …

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 …

A novel scoring function to estimate protein− ligand binding affinities has been developed
and implemented as the Glide 4.0 XP scoring function and docking protocol. In addition to …

Denaturant m values, the dependence of the free energy of unfolding on denaturant
concentration, have been collected for a large set of proteins. The m value correlates very …

Two types of noncovalent bonding interactions are present in protein structures, specific and
nonspecific. Nonspecific interactions are mostly hydrophobic and van der Waals. Specific …

Recent years have witnessed an explosion of sequence and structural information for
proteins from hyperthermophilic and thermophilic organisms. Complete genome sequences …

To understand further, and to utilize, the interactions across protein-protein interfaces, we
carried out an analysis of the hydrogen bonds and of the salt bridges in a collection of 319 …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

Here, we present the results of continuum electrostatic calculations on a dataset of 222 non-
equivalent salt bridges derived from 36 non-homologous high-resolution monomeric protein …

▪ 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 …