I will present computational and experimental evidence suggesting there exists a previously unrecognized, widespread class of monomeric protein misfolding that can explain decades-old biochemical and molecular biology data, such as how synonymous mutations can alter protein function over long time scales in vivo. That this new class of misfolding involves the formation of tertiary structural motifs (non-covalent lasso entanglements) that only recently have been recognized to occur in the majority of natively folded globular proteins. And I will provide evidence that evolutionary selection pressures have enriched non-covalent lasso entanglements in enzymes and allosteric proteins, presumably to enhance their function. Thus, the formation of these native and non-native entangled motifs are opening up new perspectives and offering new explanations to old questions.

New class of protein misfolding explains decades old biochemical data and offers new insight into protein function

Where thousands of chemistry professionals meet to share ideas and advance scientific and technical knowledge. Spring 2023 abstracts, posters, and presentations will launch at the end of March.

ACS Spring 2023

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.