Author

P. To

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· 3 Biochemistry· 2

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 5 Organism:E. coli· 4 Approach:experimental assay· 3 Assay:proteomics· 3 Approach:deep learning· 2 Assay:protein structure· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

S. D. Fried· 5 shared Y. Xia· 3 shared E. P. O'Brien· 2 shared H. E. Tarbox· 2 shared I. Sitarik· 2 shared Y. Jiang· 2 shared A. Ecer· 1 shared A. M. Bhagwat· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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5 shared papersBiophysics

S. D. Fried

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Author profile →

5 papers

Recent·Most cited

Intrinsically Disordered Regions Promote Protein Refoldability and Facilitate Retrieval from Biomolecular Condensates

P. To, A. M. Bhagwat, H. E. Tarbox, A. Ecer, H. Wendorff, Z. Jamieson, T. Trcek, S. D. Fried

The paper shows that intrinsically disordered regions (IDRs) enhance protein refoldability from denatured states and facilitate retrieval from biomolecular condensates in yeast.

bioRxiv · Jun 25, 2023 · PreprintBiochemistry

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

Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less-functional

D. A. Nissley, Y. Jiang, F. Trovato, I. Sitarik, K. Narayan, P. To, Y. Xia, S. D. Fried, E. P. O'Brien

The paper shows that misfolded proteins can bypass proteostasis by being structurally similar to native states and persisting for long periods.

bioRxiv · Aug 18, 2021Biochemistry

How synonymous mutations alter enzyme structure andfunction over long time scales

Y. Jiang, S. S. Neti, I. Sitarik, P. Pradhan, P. To, Y. Xia, S. D. Fried, S. J. Booker, E. P. O'Brien

This paper shows that synonymous mutations alter enzyme function over time by causing misfolded, entangled protein states that reduce catalytic activity.

bioRxiv · Aug 18, 2021 · PreprintBiophysics

Non-Refoldability is Pervasive Across the E. coli Proteome

P. To, B. Whitehead, H. E. Tarbox, S. D. Fried

This study shows that many E. coli proteins cannot refold properly after denaturation, suggesting that native stability is due to kinetic persistence rather than thermodynamic stability.

bioRxiv · Aug 28, 2020 · PreprintBiophysics