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 …

Small-angle scattering of X-rays (SAXS) is an established method to study the overall
structure and structural transitions of biological macromolecules in solution. For folded …

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 roles of unfolded states of proteins in normal folding and in diseases involving
aggregation, as well as the prevalence and regulatory functions of intrinsically disordered …

Elastin provides extensible tissues, including arteries and skin, with the propensity for elastic
recoil, whereas amyloid fibrils are associated with tissue-degenerative diseases, such as …

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

Small-angle X-ray scattering (SAXS) is increasingly used to characterize the structure and
interactions of biological macromolecules and their complexes in solution. Although still a …

The development of molecular descriptions of intrinsically disordered proteins (IDPs) is
essential for elucidating conformational transitions that characterize common …

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 …

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