Over the past two decades, nuclear magnetic resonance (NMR) has emerged as one of the
three principal analytical techniques used in metabolomics (the other two being gas …

Nuclear magnetic resonance (NMR) is widely employed for investigating a range of
important issues from the determination of novel molecular structures in inorganic, organic …

The emerging antibiotics-resistance problem has underlined the urgent need for novel
antimicrobial agents. Lantibiotics (lanthionine-containing antibiotics) are promising …

Despite their crucial role in the stabilization of biomolecular structures and their almost
ubiquitous involvement in biomolecular reactions, such as enzymatic cleavage or ligand …

The temperature-dependence of a large number of NMR parameters describing hydrogen
bond properties in the protein ubiquitin was followed over a range from 5 to 65° C. The …

Deprotonation or suppression of the p K a of the amino group of a lysine sidechain is a
widely recognized phenomenon whereby the sidechain amino group transiently can act as a …

The hydrogen bond (H‐bond) has been recognized in science for more than 80 years as a
concept to explain situations where a hydrogen atom is simultaneously binding to two other …

As of March 2010, 141 structures of protein–RNA complexes with a molecular weight lower
than 40 kDa have been deposited in the Protein Data Bank (PDB). Of these structures, 52 …

Hydrogen bonding plays a crucial role in Brønsted acid catalysis. However, the hydrogen
bond properties responsible for the activation of the substrate are still under debate. Here …

Conformational stability of G‐quartets found in telomeric DNA quadruplex structures
requires the coordination of monovalent ions. Here, an extensive Hartree–Fock and density …