Author

N. E. Thomas

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· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:E. coli· 2 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:drug response / drug discovery· 1 Assay:electrophysiology· 1

Frequent Co-Authors

K. A. Henzler-Wildman· 3 shared A. E. Robinson· 1 shared B. Balthazor· 1 shared C. J. Porter· 1 shared E. A. Morrison· 1 shared K. M. Hibbs· 1 shared M. Brousseau· 1 shared P. J. Spreacker· 1 shared

Activity by Year

2017-2021 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 21 mutual co-author links

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3 shared papersBiochemistry

K. A. Henzler-Wildman

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3 papers

Recent·Most cited

Activating alternative transport modes in a multidrug resistance efflux pump to confer chemical susceptibility

P. J. Spreacker, N. E. Thomas, W. F. Beeninga, M. Brousseau, C. J. Porter, K. M. Hibbs, K. A. Henzler-Wildman

The paper shows that the E. coli SMR transporter EmrE can confer susceptibility to small-molecule substrates like harmane by triggering proton uniport, leading to antibiotic synergy.

bioRxiv · Dec 4, 2021 · PreprintBiochemistry

Unlocking the reversal potential of solid supported membrane electrophysiology to determine transport stoichiometry

K. A. Henzler-Wildman, N. E. Thomas

The paper develops a new method using solid supported membrane electrophysiology to measure transport stoichiometry, verifying a 2:1 proton:guanidinium antiporter stoichiometry for Gdx.

bioRxiv · May 7, 2020 · PreprintBiochemistry

A kinetically-driven free exchange mechanism of EmrE antiport sacrifices coupling efficiency in favor of promiscuity

A. E. Robinson, N. E. Thomas, E. A. Morrison, B. Balthazor, K. A. Henzler-Wildman

This paper shows EmrE, a multidrug resistance transporter, uses a new kinetically-driven free exchange mechanism that allows promiscuous drug and proton transport, sacrificing coupling efficiency for speed and specificity.

bioRxiv · May 24, 2017Biophysics