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 …

Raman spectroscopy has become a versatile tool in protein science and biotechnology.
Recent advances in spectral assignments and vibrational theory, examples of use in …

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 …

Peptides and proteins are naturally chiral molecular systems so that sensing their structure
and conformation with chirality-based spectral methods is an obvious and long-used …

Nanoparticle chirality has attracted much attention recently, and the application of chiral
nanoparticles to chiral technologies (see figure) is also of interest. This Minireview deals …

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

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

Classical descriptions of the three‐dimensional shapes of proteins usually invoke three
main structures: α‐helix, β‐sheet, and β‐turn. More recently, the polyproline II (PPII) structure …

The poly (Pro) II (PII) conformation is increasingly recognized as an important element in
peptide and protein conformation. Circular dichroism (CD) is one of the most useful methods …

Over the last 40 years the theoretical basis has been developed for using vibrational
spectroscopy as a tool for peptide and protein structure analysis. In spite of these efforts it is …