Author

R. M. Regy

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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Research Focus:protein folding & dynamics· 3 Approach:statistical model· 3 Approach:deep learning· 2 Approach:experimental assay· 2 Assay:protein structure· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Organism:human· 1

Frequent Co-Authors

J. Mittal· 4 shared D. A. Hammer· 2 shared G. L. Dignon· 2 shared M. C. Good· 2 shared A. G. Simpkins· 1 shared A. K. Ranganath· 1 shared B. Favetta· 1 shared B. S. Schuster· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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4 shared papersBiophysics

J. Mittal

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Author profile →

4 papers

Recent·Most cited

BiophysicsbioRxivPreprintMar 10, 2023

Determinants of Disordered Protein Co-Assembly Into Discrete Condensed Phases

R. M. Welles, K. A. Sojitra, M. V. Garabedian…·M. C. Good

The paper identifies sequence determinants of IDR co-assembly into distinct condensed phases and reveals physicochemical principles governing phase separation specificity.

DOI 10.1101/2023.03.10.532134

proteomicsstatistical model

𝕏 PostBluesky

BiophysicsbioRxivMay 28, 2021

Amphiphilic proteins coassemble into multiphasic condensates and act as biomolecular surfactants

F. M. Kelley, B. Favetta, R. M. Regy…·B. S. Schuster

The paper investigates how amphiphilic proteins influence the structure and size of biomolecular condensates by forming surface layers and multiphasic structures.

DOI 10.1073/pnas.2109967118

protein structureexperimental assay

𝕏 PostBluesky

BiophysicsbioRxivAug 5, 2020

Molecular details of protein condensates probed by microsecond-long atomistic simulations

W. Zheng, G. L. Dignon, X. Xu…·J. Mittal

The paper uses all-atom simulations to study protein condensates, revealing structural and dynamic details of phase separation in two IDPs and showing agreement with experiments.

DOI 10.1021/acs.jpcb.0c10489

protein structuredeep learning

𝕏 PostBluesky

BiophysicsProceedings of the National Academy of SciencesPeer-reviewedMay 11, 2020

Identifying Sequence Perturbations to an Intrinsically Disordered Protein that Determine Its Phase Separation Behavior

B. Schuster, G. L. Dignon, W. S. Tang…·J. Mittal

This study identifies sequence features of an intrinsically disordered protein that influence its phase separation behavior through computational modeling and experimental validation.

DOI 10.1073/pnas.2000223117

humanproteomics

𝕏 PostBluesky