Peptidomimetics, non‐natural mimicries of bioactive peptides, comprise an important class
of drug molecules. The essence of the peptidomimetic design is to mimic the key …

Although the structures of native proteins are generally unique, the pathways by which they
form are often free to vary. Some proteins fold by a multitude of different pathways, whereas …

Abnormal trinucleotide repeat expansions alter protein conformation causing malfunction
and contribute to a significant number of incurable human diseases. Scarce structural …

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

The poor aqueous solubility of drug substances hampers their broader applications. This
paper describes a de novo strategy to increase the aqueous solubility of drug substances …

The structure of the first ubiquitin-associated domain from HHR23A, UBA (1), was
determined by X-ray crystallography at a 1.60 Å resolution, and its stability, folding kinetics …

Trivial trajectory parallelization of multicanonical molecular dynamics (TTP‐McMD) explores
the conformational space of a biological system with multiple short runs of McMD starting …

Polyalanine (polyA) is the third-most prevalent homopeptide repeat in eukaryotes, behind
polyglutamine and polyasparagine. Abnormal expansion of the polyA repeat is linked to at …

All-atom empirical molecular mechanics protein force fields, which have been developed to
represent the energetics of peptide folding behavior in aqueous solution, have not been …

Because the amyloid β-peptide (Aβ) functions as approximately half of the transmembrane
domain of the amyloid precursor protein and interaction of Aβ with membranes is proposed …