A proteoform is a defined form of a protein derived from a given gene with a specific amino
acid sequence and localized post‐translational modifications. In top‐down proteomic …

Contemporary protein architectures can be regarded as molecular fossils, historical imprints
that mark important milestones in the history of life. Whereas sequences change at a …

Proteins are synthesized by the ribosome and generally must fold to become functionally
active. Although it is commonly assumed that the ribosome affects the folding process, this …

Foldamer catalysis has been developed prosperously in various fields due to its enzyme-
mimic feature with admirable activity and selectivity, while there is still a blank for its …

Observations that β-sheet proteins form amyloid fibrils under at least partially denaturing
conditions has raised questions as to whether these fibrils assemble by docking of …

Models of protein folding have historically focused on a subset of 'well-behaved'proteins that
can be successfully refolded from denaturants in vitro. Energy landscapes, including folding …

Folding of polypeptides begins during their synthesis on ribosomes. This process has
evolved as a means for the cell to maintain proteostasis, by mitigating the risk of protein …

The mechanisms by which peptides and proteins form ordered aggregates are not well
understood. Here we focus on the physicochemical properties of amino acids that favor …

In living systems, polypeptide chains are synthesised on ribosomes, molecular machines
composed of over 50 protein and nucleic acid molecules. As nascent chains emerge from …

Over five decades of research have yielded a large body of information on how purified
proteins attain their native state when refolded in the test tube, starting from a chemically or …