The construction of complex protein folds relies on the precise conversion of a linear
polypeptide chain into a compact 3-dimensional structure. The interplay of forces that link …

Reverse turns are a major class of protein secondary structure; they represent sites of chain
reversal and thus sites where the globular character of a protein is created. It has been …

Transient interactions of platelet-receptor glycoprotein Ibα (GpIbα) and the plasma protein
von Willebrand factor (VWF) reduce platelet velocity at sites of vascular damage and play a …

A family of neurodegenerative diseases, including Huntington's disease (HD) and
spinocerebellar ataxias, are associated with an abnormal polyglutamine (polyQ) expansion …

Recent solid-state NMR data () demonstrate that Aβ1-40 adopts a conformation in amyloid
fibrils with two in-register, parallel β-sheets, connected by a bend structure encompassing …

A 20-residue protein (named Betanova) forming a monomeric, three-stranded, antiparallel β
sheet was designed using a structural backbone template and an iterative hierarchical …

What I cannot create, I do not understand. Richard P. Feynman β-Sheets consist of
extended polypeptide strands (β-strands) connected by a network of hydrogen bonds and …

We have studied the unfolding and refolding pathway of a β-hairpin fragment of protein G by
using molecular dynamics. Although this fragment is small, it possesses several of the …

The 62 residue IgG binding domain of protein L consists of a central α-helix packed on a four-
stranded β-sheet formed by N and C-terminal β-hairpins. The overall topology of the protein …

Both turn sequence and interstrand hydrophobic side-chain–side-chain interaction have
been suggested to be important determinants of β-hairpin stability. However, their roles in …