Though many folded proteins assume one stable structure that performs one function, a
small‐but‐increasing number remodel their secondary and tertiary structures and change …

AlphaFold2 has revolutionized protein structure prediction by leveraging sequence
information to rapidly model protein folds with atomic‐level accuracy. Nevertheless, previous …

Fold‐switching proteins, which remodel their secondary and tertiary structures in response
to cellular stimuli, suggest a new view of protein fold space. For decades, experimental …

Folded proteins are assumed to be built upon fixed scaffolds of secondary structure, α-
helices and β-sheets. Experimentally determined structures of> 58,000 non-redundant …

It has been a long-standing conviction that a protein's native fold is selected from a vast
number of conformers by the optimal constellation of enthalpically favorable interactions. In …

Metamorphic proteins constitute unexpected paradigms of the protein folding problem, as
their sequences encode two alternative folds, which reversibly interconvert within …

Extant fold‐switching proteins remodel their secondary structures and change their functions
in response to environmental stimuli. These shapeshifting proteins regulate biological …

In this study, a series of poly (amino acid) s materials with amphiphilic properties were
synthesized by ring-opening polymerization. In specific solvents, macromolecules can self …

In classical amyloidoses, amyloid fibres form through the nucleation and accretion of protein
monomers, with protofibrils and fibrils exhibiting a cross-β motif of parallel or antiparallel β …

Though typically associated with a single folded state, some globular proteins remodel their
secondary and/or tertiary structures in response to cellular stimuli. AlphaFold2 1 (AF2) …