Intramolecular NH… O, S, N interactions in non-tautomeric systems are reviewed in a broad
range of compounds covering a variety of NH donors and hydrogen bond acceptors. 1H …

NMR spectroscopy is a powerful tool for studying protein dynamics. Conventionally, NMR
studies on protein dynamics have probed motions of protein backbone NH, side-chain …

Density functional theory (DFT) and time-dependent density functional theory (TDDFT)
methods have been performed to investigate the ground and exited states intermolecular …

DNA recognition and targeting by transcription factors (TFs) through specific binding are
fundamental in biological processes. Furthermore, the histidine protonation state at the TF …

We applied a set of advanced bonding descriptors to establish the hidden electron density
features and binding energy characteristics of intermolecular D H∙∙∙ A hydrogen bonds (O …

Eukaryotic genomes contain numerous non-functional high-affinity sequences for
transcription factors. These sequences potentially serve as natural decoys that sequester …

Hydrogen bonds between protein side-chain hydroxyl (OH) and phosphate groups are one
of the most common types of intermolecular hydrogen bonds in protein–DNA/RNA …

Protein phosphorylation and glycosylation coordinately regulate numerous complex
biological processes. However, the main methods to simultaneously enrich them are based …

To perform their function, transcription factors and DNA-repair/modifying enzymes must first
locate their targets in the vast presence of nonspecific, but structurally similar sites on …

Due to chemical exchange, the mobility of histidine (His) side chains of proteins is typically
difficult to analyze by NMR spectroscopy. Using an NMR approach that is uninfluenced by …