Author

A. M. Faustino

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

S. D. Fried· 3 shared A. C. S. Rocha· 1 shared A. M. Plummer· 1 shared B. T. Amann· 1 shared D. C. Marx· 1 shared D. Yadav· 1 shared H. J. Lessen· 1 shared I. Cherepashuk· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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3 shared papersBiophysics

S. D. Fried

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3 papers

Recent·Most cited

Proteome-Wide Photo-Crosslinking Enables Residue-Level Visualization of Protein Interaction Networks in vivo

A. M. Faustino, P. Sharma, D. Yadav, S. D. Fried

This paper introduces photo-crosslinkers for proteome-wide protein interaction mapping with residue-level resolution, demonstrating their application in E. coli and showing potential for studying low-abundance proteins.

bioRxiv · Sep 20, 2022 · PreprintBiochemistry

Early selection of the amino acid alphabet was adaptively shaped by biophysical constraints of foldability

M. Makarov, A. C. S. Rocha, R. Krystufek, I. Cherepashuk, V. Dzmitruk, T. Charnavets, A. M. Faustino, M. Lebl, K. Fujishima, S. D. Fried, K. Hlouchova

This study investigates why the modern amino acid alphabet evolved to include 20 canonical amino acids by showing that foldability constraints shaped the selection of early amino acids.

bioRxiv · Jun 14, 2022Biophysics

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