Nature achieves differentiation of specific and nonspecific binding in molecular interactions
through precise control of biomolecules in space and time. Artificial systems such as …

Charged and polar groups, through forming ion pairs, hydrogen bonds, and other less
specific electrostatic interactions, impart important properties to proteins. Modulation of the …

Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

Native ESI-MS involves the transfer of intact proteins and biomolecular complexes from
solution into the gas phase. One potential pitfall is the occurrence of pH-induced changes …

Enzymes synthesized by hyperthermophiles (bacteria and archaea with optimal growth
temperatures of> 80° C), also called hyperthermophilic enzymes, are typically thermostable …

Several sequence and structural factors have been proposed to contribute toward greater
stability of thermophilic proteins. Here we present a statistical examination of structural and …

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

Techniques from graph theory are applied to analyze the bond networks in proteins and
identify the flexible and rigid regions. The bond network consists of distance constraints …

The structure, stability, solubility, and function of proteins depend on their net charge and on
the ionization state of the individual residues. Consequently, biochemists are interested in …

Salt bridges occur frequently in proteins, providing conformational specificity and
contributing to molecular recognition and catalysis. We present a comprehensive analysis of …