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 …

A typical casein micelle contains thousands of casein molecules, most of which form
thermodynamically stable complexes with nanoclusters of amorphous calcium phosphate …

The ff94 force field that is commonly associated with the Amber simulation package is one of
the most widely used parameter sets for biomolecular simulation. After a decade of …

The ensemble folding of two 21-residue α-helical peptides has been studied using all-atom
simulations under several variants of the AMBER potential in explicit solvent using a global …

Under physiological conditions, a protein undergoes a spontaneous disorder⇌ order
transition called “folding.” The protein polymer is highly flexible when unfolded but adopts its …

We seek to understand the link between protein thermodynamics and protein structure in
molecular detail. A classical approach to this problem involves assessing changes in protein …

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 Gaussian-distributed random coil has been the dominant model for denatured proteins
since the 1950s, and it has long been interpreted to mean that proteins are featureless …

The first crystal structure of an oligoproline adopting an all-trans polyproline II (PPII) helix is
presented. The high-resolution structure provides detailed insight into the dimensions and …

Force-field validation is essential for the identification of weaknesses in current models and
the development of more accurate models of biomolecules. NMR coupling and relaxation …