A protein is usually classified into one of the following five structural classes: α, β, α+ β, α/β,
and ζ (irregular). The structural class of a protein is correlated with its amino acid …

Helix‐capping motifs are specific patterns of hydrogen bonding and hydrophobic
interactions found at or near the ends of helices in both proteins and peptides. In an α‐helix …

Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local
conformation, and homologous proteins show quite similar patterns of secondary chemical …

A novel folding motif has been observed in four different proteins which bind
oligonucleotides or oligosaccharides: staphylococcal nuclease, anticodon binding domain …

For unstructured “randomcoil” peptides it has long been recognized that the chemical shift of
the Ca and side-chain carbons of a given residue is largely independent of the nature of …

Abstract Three‐dimensional (3D) domain swapping creates a bond between two or more
protein molecules as they exchange their identical domains. Since the term'3D domain …

Abstract 3D domain swapping is a mechanism for forming oligomeric proteins from their
monomers. In 3D domain swapping, one domain of a monomeric protein is replaced by the …

Many biological molecules contain phosphate or sulfate, and the enzymatic reactions that
transfer these groups play important roles in metabolism. DNA and RNA are phosphate …

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 …

Specific side-by-side interactions between transmembrane alpha-helices may be important
in the assembly and function of integral membrane proteins. We describe a system for the …