The discovery of Intrinsically Disordered Proteins, which contain significant levels of disorder
yet perform complex biologically functions, as well as unwanted aggregation, has motivated …

Several lines of evidence now well establish that unfolded peptides in general, and alanine
in specific, have an intrinsic preference for the polyproline II (pPII) conformation …

Molecular dynamics (MD) is a powerful tool for studying intrinsically disordered proteins,
however, its reliability depends on the accuracy of the force field. We assess Amber ff19SB …

Conformational preferences of amino acid residues in water are determined by the
backbone and side-chain properties. Alanine is known for its high polyproline II (pPII) …

We extensively mapped energy landscapes and conformations of 22 (including three His
protonation states) proteinogenic α-amino acids in trans configuration and the …

Intrinsically disordered proteins and intrinsically disordered regions are frequently enriched
in charged amino acids. Intrinsically disordered regions are regularly involved in important …

The cationic tripeptide GAG undergoes three conformational changes in binary mixtures of
water and ethanol. At 17 mol% of ethanol conformational sampling is shifted from pPII …

We performed a conformational analysis of the central residues of three tripeptides glycyl‐l‐
isoleucyl‐glycine (GIG), glycyl‐l‐tyrosyl‐glycine (GYG) and glycyl‐l‐arginyl‐glycine (GRG) in …

Growing evidence suggests that the conformational distributions of amino acid residues in
unfolded peptides and proteins depend on the nature of the nearest neighbors. To explore …

The conformational propensity of amino acid residues is determined by an intricate balance
of peptide–solvent and solvent–solvent interactions. To explore how the systematic …