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Published in 2023 at "Protein Science"
DOI: 10.1002/pro.4596
Abstract: 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 their functions in response to cellular stimuli. These fold‐switching proteins regulate biological…
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Keywords:
distinguishing features;
fold switching;
intrinsically disordered;
fold switchers ... See more keywords
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Published in 2025 at "Protein Science"
DOI: 10.1002/pro.70329
Abstract: The mitotic arrest deficiency 2 (MAD2) exists in inactive and active forms under physiologic conditions. In its active conformation, MAD2 binds to the cell division cycle protein 20 (Cdc20) and prevents the separation of duplicated…
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Keywords:
protein;
fold switching;
energy landscape;
mad2 ... See more keywords
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Published in 2025 at "Journal of chemical information and modeling"
DOI: 10.1021/acs.jcim.5c01435
Abstract: Structural plasticity of naturally occurring proteins allows them to change their shape in response to environmental factors such as pH, temperature, or binding partners. This ability to adopt different conformations is essential for many biological…
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Keywords:
sequence similarity;
design;
protein sequences;
fold switching ... See more keywords
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Published in 2025 at "Bioinformatics"
DOI: 10.1093/bioinformatics/btaf635
Abstract: Abstract Motivation Functionally important ‘fold-switching’ proteins, which do not obey the classical folding dogma, are now thought to be widespread. Algorithms that can accurately annotate fold-switching proteins from sequence information can help uncover the true…
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Keywords:
fragment based;
switching behaviour;
morpheus fragment;
fold switching ... See more keywords