We have analysed the frequency with which potential hydrogen bond donors and acceptors
are satisfied in protein molecules. There are a small percentage of nitrogen or oxygen atoms …

We investigate the suggestion that aromatic rings can act as hydrogen-bond acceptors in
proteins, by an analysis of 55 non-homologous high-resolution protein chain structures …

Evidence from proteins and peptides supports the conclusion that intrapeptide hydrogen
bonds stabilize the folded form of proteins. Paradoxically, evidence from small molecules …

Why does a given protein structure form and why is this structure stable? These fundamental
biochemical questions remain fascinating and challenging problems because the physical …

A global census of the hydrogen bonds in 42 X-ray-elucidated proteins was taken and the
following demographic trends identified:(1) Most hydrogen bonds are local, ie between …

The structure of human lysozyme has been crystallographically refined at 1.5 Å resolution by
difference map and restrained least-squares procedures to an R factor of 0.187. A …

An analysis of the various parameters associated with N‐H… O type of hydrogen bonds has
been made using data from reported crystal structures of amino acids and simple peptides …

Hydrogen bonds are a major feature of protein structure. By a generally accepted definition,
they occur whenever a proton is shared by two electronegative atoms. Hence, only …

We have compared hydrogen bond lengths on enzymes derived with high precision
(≤±0.05 Å) from both the proton chemical shifts (δ) and the fractionation factors (ϕ) of the …

The characteristics of N H··· O, O H··· O, and C H··· O hydrogen bonds and other weak
intermolecular interactions are analyzed in a large and diverse group of 251 protein–ligand …