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 …

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 …

The program SSDraw generates publication‐quality protein secondary structure diagrams
from three‐dimensional protein structures. To depict relationships between secondary …

The Zα fold specifically binds to both Z-DNA and Z-RNA, left-handed nucleic acid structures
that form under physiological conditions and are encoded by flipons. I trace the Zα fold back …

Although most globular proteins fold into a single stable structure, an increasing number
have been shown to remodel their secondary and tertiary structures in response to cellular …

During protein evolution, some amino acid substitutions modulate protein function
(“tuneability”). In most proteins, the tuneable range is wide and can be sampled by a set of …

Numerous molecular machines are required to drive the central dogma of molecular biology.
However, the means by which these numerous proteins emerged in the early evolutionary …

Metamorphic proteins switch reversibly between multiple distinct, stable structures, often
with different functions. It was previously hypothesized that metamorphic proteins arose as …

Understanding the conformational dynamics of proteins, such as the inward-facing (IF) and
outward-facing (OF) transition observed in transporters, is vital for elucidating their functional …

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 …