The functional properties of a protein primarily depend on its three-dimensional (3D)
structure. These properties have classically been assigned, visualized and analysed on the …

Protein loops connect regular secondary structures and contain 4-residue beta turns which
represent 63% of the residues in loops. The commonly used classification of beta turns …

Background Secondary structures are elements of great importance in structural biology,
biochemistry and bioinformatics. They are broadly composed of two repetitive structures …

A protein backbone has two degrees of conformational freedom per residue, described by its
φ, ψ-angles. Accordingly, the energy landscape of a blocked peptide unit can be mapped in …

The Ramachandran map clearly delineates the regions of accessible conformational (φ–ψ)
space for amino acid residues in proteins. Experimental distributions of φ, ψ values in high …

The Ramachandran plot for backbone ϕ, ψ‐angles in a blocked monopeptide has played a
central role in understanding protein structure. Curiously, a similar analysis for side chain χ …

An exhaustive umbrella sampling simulation of the alanine dipeptide in solution is reported.
The presence of stable Y conformations in solution is assessed by both quantum …

Experimentally derived, amino acid specific backbone dihedral angle distributions are
invaluable for modeling data-driven conformational equilibria of proteins and for enabling …

It is often assumed that the peptide backbone forms a substantial number of additional
hydrogen bonds when a protein unfolds. We challenge that assumption in this article. Early …

To advance our understanding of protein tertiary structure, the development of the knob‐
socket model is completed in an analysis of the packing in irregular coil and turn secondary …