Jerelle Joseph

Assistant Professor

Princeton University

United States

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Jerelle Joseph is an Assistant Professor at Princeton University in the United States. His research focuses on the thermoresponsive phase behavior of proteins, molecular charge asymmetry in condensate size control, and the partitioning of small molecules into biomolecular condensates. He has published various articles exploring the microstructure and functional properties of engineered biomolecular condensates and has contributed to understanding the dynamics of prion-like domains.

Articles (20)

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2021

Collaborators (5)

Yi Shen

Lecturer / Assistant Professor

University of Sydney

AUSTRALIA

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Rosana Collepardo-Guevara

University of Cambridge

UNITED KINGDOM

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Ignacio Sanchez-Burgos

University of Cambridge

UNITED KINGDOM

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Virginia Jiang

Princeton University

UNITED STATES

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Stephen Farr

University of Edinburgh

UNITED KINGDOM

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Jerelle Joseph

Research Interests

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About

Articles (20)

Maltodextrin transport in the extremely thermophilic, lignocellulose degrading bacterium Anaerocellum bescii (f. Caldicellulosiruptor bescii )

Accurate prediction of thermoresponsive phase behavior of disordered proteins

Theory of Condensate Size Control by Molecular Charge Asymmetry

Prediction of Small-Molecule Partitioning into Biomolecular Condensates from Simulation

Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function

Decoding phase separation of prion-like domains through data-driven scaling laws

Decoding phase separation of prion-like domains through data-driven scaling laws

Biomolecular condensate microstructure is invariant to sequence-encoded molecular and macroscopic properties

Tandem-repeat proteins introduce tuneable properties to engineered biomolecular condensates

Accelerated Simulations Reveal Physicochemical Factors Governing Stability and Composition of RNA Clusters

Energy landscapes and heat capacity signatures for peptides correlate with phase separation propensity

Thermodynamic origins of two-component multiphase condensates of proteins

RNA length has a non-trivial effect in the stability of biomolecular condensates formed by RNA-binding proteins

Aging can transform single-component protein condensates into multiphase architectures

Surface Electrostatics Govern the Emulsion Stability of Biomolecular Condensates

Thermodynamics and kinetics of phase separation of protein-RNA mixtures by a minimal model

Valency and Binding Affinity Variations Can Regulate the Multilayered Organization of Protein Condensates with Many Components

Physics-driven coarse-grained model for biomolecular phase separation with near-quantitative accuracy

Nucleosome plasticity is a critical element of chromatin liquid–liquid phase separation and multivalent nucleosome interactions

Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions

Collaborators (5)

Yi Shen

Rosana Collepardo-Guevara

Ignacio Sanchez-Burgos

Virginia Jiang

Stephen Farr

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