Cellular function depends on highly specific interactions between biomolecules (proteins,
RNA, DNA, and carbohydrates). A basic limitation of drug development is the inability of …

Examination of complexes of proteins with other biomolecules reveals that proteins tend to
interact with partners via folded subdomains, in which the backbone possesses secondary …

Chimeric fusion proteins are essential tools for protein nanotechnology. Non-optimized
protein-protein connections are usually flexible and therefore unsuitable as structural …

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 …

Highlights•We highlight recent development of small-molecule α-helix mimetics.•We review
solid-phase synthesis of small-molecule α-helix mimetics.•We highlight HTS methods for the …

The specificity of intracellular signaling events is controlled, in part, by compartmentalization
of protein kinases and phosphatases. The subcellular localization of these enzymes is often …

The stabilization of protein–protein interactions (PPIs) has emerged as a promising strategy
in chemical biology and drug discovery. The identification of suitable starting points for …

Mechanically stable specific heterodimerization between small protein domains have a wide
scope of applications, from using as a molecular anchorage in single-molecule force …

Helix-loop-helix (HLH) and helix-loop-helix-leucine zipper (HLHZip) are dimerization
domains that mediate selective pairing among members of a large transcription factor family …

Miniproteins simplify the protein-folding problem, allowing the dissection of forces that
stabilize protein structures. Here we describe PPα-Tyr, a designed peptide comprising an α …