The poly-l-proline type II (PPII) helix in recent years has emerged clearly as a structural class
not only of fibrillar proteins (in collagen, PPII is a dominant conformation) but also of the …

Despite its theoretical and practical importance, protein folding remains among the most
fundamental unsolved problems in the life sciences. The challenge of predicting folded …

The existence and functioning of intrinsically disordered proteins (IDPs) challenge the
classical structure-function paradigm that equates function with a well-defined 3D structure …

The ϕ, ψ backbone angle distribution of small homopolymeric model peptides is
investigated by a joint molecular dynamics (MD) simulation and heteronuclear NMR study …

The polyproline type II (PPII) helix is a prevalent conformation in both folded and unfolded
proteins, and is known to play important roles in a wide variety of biological processes …

There is growing appreciation of the functional relevance of unfolded proteins in biology.
However, unfolded states of proteins have proven inaccessible to the usual techniques for …

Type II polyproline helices (PPII) are a fundamental secondary structure of proteins, common
in globular and nonglobular regions and important in cellular signaling. We developed a …

The use of parallel tempering or replica exchange molecular dynamics (REMD) simulations
has facilitated the exploration of free energy landscapes for complex molecular systems, but …

The alanine-based peptide Ac-XX (A) 7OO-NH2, referred to as XAO (where X, A, and O
denote diaminobutyric acid, alanine, and ornithine, respectively), has recently been …

A reliable intrinsic propensity scale of amino acid residues is indispensable for an
assessment of how local conformational distributions in the unfolded state can affect the …