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 …

Proline is an anomalous amino acid. Its nitrogen atom is covalently locked within a ring, thus
it is the only proteinogenic amino acid with a constrained phi angle. Sequences of three …

The mucosal glycocalyx of the ocular surface constitutes the point of interaction between the
tear film and the apical epithelial cells. Membrane-associated mucins (MAMs) are the …

Five peptides previously suggested to possess polyproline II (PPII) structure have here been
investigated by using atomistic molecular dynamics simulations to compare how well four …

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 …

The class II region of the major histocompatibility complex (MHC) locus is the main
contributor to the genetic susceptibility to type 1 diabetes (T1D). The loss of an aspartic acid …

Phosphorylation is a common post-translational modification among intrinsically disordered
proteins and regions, which helps regulate function by changing the protein conformations …

Aggregation of monomeric amyloid β peptides (Aβ) into soluble oligomers and insoluble
fibrils is one of the major pathological hallmarks of Alzheimer s disease (AD).[1] In the past …

Predicting the binding affinity of peptides able to interact with major histocompatibility
complex (MHC) molecules is a priority for researchers working in the identification of novel …

Miniproteins simplify the protein-folding problem, allowing the dissection of forces that
stabilize protein structures. Here we describe PPα-Tyr, a designed peptide comprising an α …