Author

A. M. Zmyslowski

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Research Focus:chromatin & epigenetic regulation· 1 Organism:E. coli· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Assay:proteomics· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

T. R. Sosnick· 2 shared I. A. Gagnon· 1 shared J. A. Riback· 1 shared K. W. Plaxco· 1 shared M. A. Bowman· 1 shared M. C. Baxa· 1 shared P. L. Clark· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

7 top collaborators · 13 mutual co-author links

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2 shared papersBiochemistry

T. R. Sosnick

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2 papers

Recent·Most cited

HDX-MS performed on BtuB in E. coli outer membranes delineates the luminal domain's allostery and unfolding upon B12 and TonB binding

A. M. Zmyslowski, M. C. Baxa, I. A. Gagnon, T. R. Sosnick

This study uses HDX-MS on BtuB in E. coli outer membranes to show B12 binding destabilizes the Ionic Lock, while TonB binding has weaker effects and no pore formation is observed.

bioRxiv · Jan 7, 2022Biochemistry

Commonly-used FRET fluorophores promote collapse of an otherwise disordered protein.

J. A. Riback, M. A. Bowman, A. M. Zmyslowski, K. W. Plaxco, P. L. Clark, T. R. Sosnick

The paper shows that FRET fluorophores can cause disordered proteins to contract, explaining discrepancies between FRET and SAXS measurements of unfolded proteins.

bioRxiv · Oct 31, 2018Biophysics