John P. Orban

This study identifies the flexible N-terminal domain of Sorcin as a critical regulator that enhances Ca2+ responsiveness by stabilizing its active conformation through dynamic contacts.

This study benchmarks deep learning models' ability to predict mutation-induced fold switching in proteins using an NMR-characterized dataset of fold-switching mutants.

This paper demonstrates that engineered RASProtease degrades active KRAS in cancer cells, leading to reduced MEK-ERK signaling and significant cell death in KRAS-dependent MIA PaCa-2 cells.

This paper shows how substrate specificity in a designed RAS-targeting protease is linked to active site and distal motions, revealing mechanisms for enhanced specificity.

The paper identifies cold-sensitive protein conformational changes across the proteome using mass spectrometry in E. coli.

This study reveals the conformational dynamics of Paxillin's N-domain interacting with FAK's FAT domain, showing a multi-state complex with functional implications.