Author

I. Sitarik

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 Biochemistry· 1

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Research Focus:protein folding & dynamics· 5 Organism:E. coli· 4 Assay:protein structure· 4 Approach:statistical model· 4 Approach:deep learning· 3 Approach:experimental assay· 1 Assay:protein sequence· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

E. P. O'Brien· 5 shared D. A. Nissley· 3 shared S. D. Fried· 3 shared Y. Jiang· 3 shared M. S. Li· 2 shared P. To· 2 shared Y. Xia· 2 shared D. Yadav· 1 shared

Activity by Year

2021-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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5 shared papersBiophysics

E. P. O'Brien

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5 papers

Recent·Most cited

A Newly Identified Class of Protein Misfolding in All-atom Folding Simulations Consistent with Limited Proteolysis Mass Spectrometry

Q. V. Vu, I. Sitarik, Y. Jiang, D. Yadav, P. Sharma, S. D. Fried, M. S. Li, E. P. O'Brien

The paper identifies entangled misfolded states in all-atom protein folding simulations that resemble native states and are consistent with mass spectrometry data.

bioRxiv · Jul 19, 2022 · PreprintBiophysics

Synonymous mutations can alter protein dimerization through localized interface misfolding involving self-entanglements

L. P. Dang, D. A. Nissley, I. Sitarik, Q. V. Van, Y. A. Jiang, M. S. Li, E. P. O'Brien

This paper shows synonymous mutations can alter protein dimerization by causing misfolded self-entangled states that disrupt dimer interfaces, with effects dependent on translation speed.

bioRxiv · Oct 26, 2021Biophysics

Subpopulations of soluble, misfolded proteins commonly bypass chaperones: How it happens at the molecular level

R. Halder, D. A. Nissley, I. Sitarik, E. P. O'Brien

The paper shows that some soluble, misfolded proteins evade chaperones by being structurally similar to native states, leading to long-term misfolding.

bioRxiv · Aug 18, 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