Abstract Motivation Polyproline II (PPII) is a common conformation, comparable to α-helix
and β-sheet. PPII, recently termed with a more generic name—κ-helix, adopts a left-handed …

Motivation More than half of the human proteome contains the proline-rich motif, PxxP. This
motif has a high propensity for adopting a left-handed polyproline II (PPII) helix and can …

Despite the clear importance of the left‐handed polyproline II (PPII) helical conformation in
many physiologically important processes as well as its potential significance in protein …

Texas A&M Univ, College Station, TX, USA. The 136 kDa Bacillus stearothermophilus
phosphofructokinase (BsPFK) is a homotetramer that is allosterically inhibited by phospho …

Glycine rich polyproline II helix assemblies are an emerging class of natural domains found
in several proteins with different functions and diverse origins. The distinct properties of …

Although not being classified as the most fundamental protein structural elements like α-
helices and β-strands, the loop segment may play considerable roles for protein stability …

Protein science is being transformed by powerful computational methods for structure
prediction and design: AlphaFold2 can predict many natural protein structures from …

Poly-proline fragments form the distinctive PPII-helix in a high percentage in proteins and
peptides, which plays an important role in signal transduction and protein complex …

Canonical π-helices are short, relatively unstable secondary structure elements found in
proteins. They comprise seven or more residues and are present in 15% of all known protein …

Beta turns, in which the protein backbone abruptly changes direction over four amino acid
residues, are the most common type of protein secondary structure after helices and strands …