Fold-switching proteins respond to cellular stimuli by remodeling their secondary structures
and changing their functions. Whereas several previous reviews have focused on various …

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 …

Metamorphic proteins switch between different folds, defying the protein folding paradigm. It
is unclear how fold switching arises during evolution. With ancestral reconstruction and …

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 …

Metamorphic proteins are single amino acid sequences that reversibly interconvert between
multiple, dramatically different native structures, often with distinct functions. Since the …

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 …

Nanotechnology is an expanding field with significant potential to benefit society. This study
focuses on the environmentally friendly synthesis of copper oxide nanoparticles (CuONPs) …

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 …

Four de novo proteins differing in single mutation positions, with a chain length of 56 amino
acids, represent diverse 3D structures: monomeric 3α and 4β+ α folds. The reason for this …