The deshielding or downfield 13C NMR chemical shift of amide carbonyl carbon upon H‐
bonding is a widely observed phenomenon. This downfield shift is commonly used as a …

Nature makes extensive and elaborate use of hydrogen bonding to assemble and stabilize
biomolecular structures. The shapes of peptides and proteins rely significantly on N–H⋯ OC …

One of the most familiar carbon-centered noncovalent interactions (NCIs) involving an
antibonding π*-orbital situated at the Bürgi–Dunitz angle from the electron donor, mostly …

Hydrogen bonds (H-bonds) are ubiquitous in peptides and proteins and are central to the
stabilization of their structures. Inter-residue H-bonds between non-adjacent backbone …

Detection and removal of metal ion contaminants have attracted great interest due to the
health risks that they represent for humans and wildlife. Among the proposed compounds …

The δ conformation is a local secondary structure in proteins that implicates a πamide N–H⋯
N interaction between a backbone N atom and the NH of the following residue. Small …

New Cδ–H⋯ O histidine hydrogen bonding interactions in various proteins are identified by
neutron diffraction and computationally characterized. Neutron diffraction data shows …

Abstract Models of asparagine‐containing dipeptides specifically designed to favor intrinsic
folding into an Asx turn were characterized both theoretically, by using quantum chemistry …

Folding motifs of the secondary structures of peptides and proteins are primarily based on
the hydrogen bonding interactions in the backbone as well as the sequence of the amino …

We examine peptide model systems designed to probe short-range N–H⋯ OS sidechain–
backbone hydrogen bonding involving amino acid residues with sidechain sulfoxide or …