Author

W. M. Borcherds

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· 7

Signature Assays, Organisms & Methods

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Approach:statistical model· 4 Research Focus:cell type annotation· 3 Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Assay:protein sequence· 2 Research Focus:chromatin & epigenetic regulation· 1 Assay:imaging· 1 Assay:protein structure· 1

Frequent Co-Authors

R. V. Pappu· 6 shared T. Mittag· 6 shared A. Bremer· 5 shared M. Farag· 5 shared A. E. Posey· 2 shared S. R. Cohen· 2 shared A. Barozet· 1 shared A. Estana· 1 shared

Activity by Year

2021-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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6 shared papersBiophysics

R. V. Pappu

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7 papers

Recent·Most cited

Optical characterization of molecular interaction strength in protein condensates

T. Beck, L.-M. van der Linden, W. M. Borcherds, K. Kim, R. Schluessler, P. Mueller, T. Franzmann, C. Moeckel, R. Goswami, M. Leaver, T. Mittag, S. Alberti, J. Guck

The paper introduces optical techniques to measure molecular interaction strength and physical properties of protein condensates, showing how sequence variations and environmental factors affect these properties.

bioRxiv · Mar 19, 2024Biophysics

Sequence-specific interactions determine viscoelasticity and aging dynamics of protein condensates

I. Alshareedah, W. M. Borcherds, S. R. Cohen, A. Singh, A. E. Posey, M. Farag, A. Bremer, G. W. Strout, D. T. Tomares, R. V. Pappu, T. Mittag, P. R. Banerjee

This study investigates how sequence-specific interactions influence the viscoelastic properties and aging dynamics of protein condensates formed by prion-like low-complexity domains.

bioRxiv · Apr 6, 2023Biophysics

Phase Separation in Mixtures of Prion-Like Low Complexity Domains is Driven by the Interplay of Homotypic and Heterotypic Interactions

M. Farag, W. M. Borcherds, A. Bremer, T. Mittag, R. V. Pappu

This paper investigates phase separation of mixtures of prion-like low complexity domains using simulations and experiments, finding that homotypic and heterotypic interactions drive condensate formation.

bioRxiv · Mar 15, 2023 · PreprintBiophysics

Quantifying coexistence concentrations in multi-component phase-separating systems using analytical HPLC

A. Bremer, A. E. Posey, M. B. Borgia, W. M. Borcherds, M. Farag, R. V. Pappu, T. Mittag

This paper develops an analytical HPLC method to quantify coexisting phase concentrations in multi-component phase-separating systems, enabling reconstruction of coexistence curves.

bioRxiv · Sep 11, 2022Biophysics

Condensates of disordered proteins have small-world network structures and interfaces defined by expanded conformations

M. Farag, S. R. Cohen, W. M. Borcherds, A. Bremer, T. Mittag, R. V. Pappu

This study shows that disordered protein condensates form small-world networks with interface-specific conformational expansions and orientations.

bioRxiv · May 21, 2022 · PreprintBiophysics

Conformational buffering underlies functional selection in intrinsically disordered protein regions

N. S. Gonzalez-Foutel, W. M. Borcherds, J. Glavina, S. Barrera-Vilarmau, A. Sagar, A. Estana, A. Barozet, G. Fernandez-Ballester, C. Blanes-Mira, I. E. Sanchez, G. de Prat Gay, J. Cortes, P. Bernado, R. V. Pappu, A. S. Holehouse, , L. B. Chemes

The paper identifies conformational buffering as a mechanism that conserves spatial dimensions in disordered protein regions despite sequence variation, enabling functional selection.

bioRxiv · May 14, 2021Biophysics

Deciphering how naturally occurring sequence features impact the phase behaviors of disordered prion-like domains

A. Bremer, M. Farag, W. M. Borcherds, I. Peran, E. W. Martin, R. V. Pappu, T. Mittag

The paper identifies how specific amino acid compositions influence phase separation in prion-like domains and develops a model to simulate these behaviors.

bioRxiv · Jan 1, 2021Biophysics