Author

T. Devlin

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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Biophysics· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Organism:E. coli· 1 Assay:proteomics· 1 Approach:simulation· 1 Approach:statistical model· 1

Frequent Co-Authors

K. G. Fleming· 4 shared A. M. Plummer· 2 shared D. C. Marx· 2 shared M. A. Roskopf· 2 shared P. J. Fleming· 2 shared S. D. Fried· 2 shared A. M. Faustino· 1 shared B. T. Amann· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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4 shared papersBiophysics

K. G. Fleming

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Author profile →

4 papers

Recent·Most cited

FkpA Enhances Membrane Protein Folding using an Extensive Interaction Surface

T. Devlin, D. C. Marx, M. A. Roskopf, Q. R. Bubb, A. M. Plummer, K. G. Fleming

This study investigates FkpA's role in enhancing outer membrane protein folding and shows it binds clients with an extensive interface, distinct from other chaperones.

bioRxiv · Nov 1, 2022Biophysics

Generation of Unfolded Outer Membrane Protein Ensembles Targeted by Hydrodynamic Properties

T. Devlin, P. J. Fleming, N. Loza, K. G. Fleming

The paper models unfolded outer membrane protein ensembles using experimental data and simulations to understand their conformational differences.

bioRxiv · Oct 31, 2022 · PreprintBiophysics

A Proteome-Wide Map of Chaperone-Assisted Protein Refolding in the Cytosol

P. To, S. O. Lee, Y. Xia, T. Devlin, K. G. Fleming, S. D. Fried

This study maps chaperone-assisted protein refolding in E. coli cytosol using mass spectrometry, showing GroEL refolds most proteins and identifies intransigent proteins that fold co-translationally.

bioRxiv · Nov 20, 2021 · PreprintBiophysics

SurA is a "Groove-y" Chaperone That Expands Unfolded Outer Membrane Proteins

D. C. Marx, A. M. Plummer, A. M. Faustino, M. A. Roskopf, M. J. Leblanc, T. Devlin, H. J. Lessen, B. T. Amann, P. J. Fleming, S. Krueger, S. D. Fried, K. G. Fleming

This paper investigates how SurA, a bacterial chaperone, interacts with unfolded outer membrane proteins (uOMPs) using structural biology techniques, revealing distinct binding modes and a mechanism for uOMP expansion.

bioRxiv · Dec 17, 2019Biophysics