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The Komives lab pioneered using hydrogen deuterium exchange to map protein-protein interfaces by HDX-MS. Combining HDX-MS with NMR and single molecule FRET allowed them to address important but unsolved questions about allosteric regulation of proteins. Initial discoveries focused on the biophysical behavior of thrombin:thrombomodulin complexes. They discovered that thrombomodulin alters the dynamic ensemble of thrombin to favor the catalytically active state. It furthermore induces motions on multiple timescales linked to catalysis. Work on NFB-IB signaling established an original paradigm demonstrating kinetic control of transcription factor dynamics. Here, single molecule FRET was used to demonstrate slow timescale motions that expose the IκBα degron and that expose NFκB to facilitated dissociation from the DNA mediated by IκBα. In another project, we uncovered allostery through a 10-protein ubiquitin E3 ligase complex. In this complex, an ankyrin repeat protein and Cullin 5 each act as a rigid rod connecting the substrate binding site to the ubiquitylation machinery. The lab utilizes a broad range of biophysical tools to discover new principles, which have profoundly advanced our fundamental understanding of macromolecular recognition.
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The Journal of Physical Chemistry Bno. 24 (2024): 5803-5813
Daniel J. Brogan,Elena Dalla Benetta, Tianqi Wang,Calvin P. Lin, Fangying Chen, Harry Li, Claire Lin,Elizabeth A. Komives,Omar S. Akbari
biorxiv(2024)
Biochemistryno. 11 (2024): 1434-1444
Matthew Mealka, Nicole A. Sierra,Diego Avellaneda Matteo, Elene Albekioni, Rachel Khoury, Timothy Mai, Brittany M. Conley,Nalani J. Coleman,Kaitlyn A. Sabo,Elizabeth A. Komives,Andrey A. Bobkov,Andrew L. Cooksy,
PROTEIN SCIENCEno. 12 (2023)
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Methods (San Diego, Calif.) (2023): 18-25
NATURE COMMUNICATIONSno. 1 (2023)
Journal of Biological Chemistryno. 3 (2023): S299-S300
Biochemical Society transactionsno. 6 (2023): 2085-2092
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