ER/K α-helices are a subset of single alpha helical domains, which exhibit unusual stability
as isolated protein secondary structures. They adopt an elongated structural conformation …

Assessment of helical interfaces in protein – protein interactions - Molecular BioSystems (RSC
Publishing) DOI:10.1039/B903202A Royal Society of Chemistry View PDF VersionPrevious …

Cellular functions of proteins are strongly influenced by their interactions with other proteins.
The frequency of protein interactions is a function of the local concentration of two proteins …

The α-helix is a ubiquitous secondary structural element that is almost exclusively observed
in proteins when stabilized by tertiary or quaternary interactions. However, beginning with …

The α-helix is one of the most common protein surface recognition motifs found in nature,
and its unique amide-cloaking properties also enable α-helical polypeptide motifs to exist in …

The development of inhibitors for protein–protein interactions frequently involves the mimicry
of secondary structure motifs. While helical protein–protein interactions have been heavily …

Protein–protein interactions play critical roles in a wide variety of biological processes, and
their dysregulations contribute to the pathogenesis of several diseases, including cancer …

Protein α-helices are ubiquitous secondary structural elements, seldom considered to be
stable without tertiary contacts. However, amino acid sequences in proteins that are based …

Naturally-occurring single α-helices (SAHs), are rich in Arg (R), Glu (E) and Lys (K) residues,
and stabilized by multiple salt bridges. Understanding how salt bridges promote their …

The eukaryotic cell is a bustling collection of macromolecules acting cooperatively to
mediate the functions required for cell viability. Specific, context-dependent and tightly …