About

Jerelle A. Joseph is an Assistant Professor of Chemical and Biological Engineering at Princeton University and a member of the Omenn-Darling Bioengineering Institute. His research focuses on understanding the principles governing intracellular compartmentalization, particularly biomolecular condensates—cell compartments composed of proteins, RNA, and other biomolecules that assemble via phase separation. These condensates are linked to normal cellular functions such as RNA processing, as well as to disorders like neurodegenerative diseases, cancers, and infectious diseases. His work aims to characterize the physicochemical factors that determine the formation, dissolution, and misregulation of these condensates, with the goal of engineering new cellular functions and developing therapeutic strategies.

Research topics

• Chemistry
• Chemical physics
• Biophysics
• Biology
• Physics
• Computer Science
• Thermodynamics
• Computational chemistry
• Cell biology
• Statistical physics
• Organic chemistry
• Biological system
• Biochemistry

Selected publications

• Non-equilibrium modeling of directed flux through biomolecular condensates

  bioRxiv (Cold Spring Harbor Laboratory) · 2026-02-06 · 1 citations

  articleOpen accessSenior authorCorresponding

  Cellular biomolecular condensates function far from equilibrium, sustained by continuous influx and efflux of molecular components. Notable examples include the nucleolus, nuclear pore complex, P-bodies, and stress granules, in which regulated molecular transport is essential for their function. Experimental characterization of molecular flux remains challenging due to limitations in spatiotemporal resolution, making computational approaches a powerful alternative for systematic investigation. Here, we present a computational approach (TRACE) to model molecular transport through biomolecular condensates under non-equilibrium steady-state conditions at near-atomistic resolution. Using TRACE, we systematically probe physicochemical factors that govern molecular flux through condensates. We find that protein sequence composition and patterning determine the internal structure of the condensates, which strongly influences molecular transport efficiency. Our work also suggests that molecular flux through condensates exhibits reptation dynamics. Moreover, interactions between fluxing molecules and condensates play a critical role in regulating transport. In particular, associative interactions enable a ‘handoff mechanism’, in which successive transient interactions facilitate directed transport through condensates. Together, these results help advance our understanding on how molecular flux is regulated in biomolecular condensates and provide a basis for rationally tuning condensate-mediated molecular flux, with potential applications in therapeutics and active soft material design.

  PublisherDOI

• Molecular origins of viscoelasticity in biomolecular condensates

  The Journal of Chemical Physics · 2026-02-11

  articleOpen accessSenior author

  Biomolecular condensates are membraneless organelles that compartmentalize functions in living cells. Formed by the phase separation of biomolecules, condensates possess a wide range of mechanical responses. However, how condensate viscoelastic response is encoded in the chemistries of their constituents-such as intrinsically disordered proteins (IDPs)-is not well understood. Here, we employ molecular dynamics simulations to connect measurable condensate viscoelasticity to the architectural heterogeneity and dynamic reconfigurability of associative networks formed by IDPs. Using a residue-resolution coarse-grained model, we characterize biologically relevant and synthetic condensates, demonstrating that the temperature sensitivity of elasticity is sequence-dependent and modeled by exponential scaling laws. We interrogate condensate mesh heterogeneity via entanglement spacing, finding that entropy-driven structural heterogeneity and reduced IDP hydrophobicity favor condensate elasticity. Furthermore, we construct graph-theoretical representations of condensates and find that interaction network topologies with an abundance of redundant node pathways translate to more load-bearing paths for mechanical stress storage. Strikingly, we discover that elastic coupling of IDPs within condensates emerges when single-molecule shape memory timescales approach mesh reconfiguration timescales. This interplay of timescales for molecular and microstructural processes, which we introduce as the condensate Deborah number, dictates how restoring elastic forces propagate and are stored across IDP networks, linking condensate microstructure dynamics directly to mechanical responses. Taken together, our work provides a conceptual framework of how condensates act as stress-responsive biomaterials, helping illuminate how cells exploit condensate mechanics to sense and regulate their internal environment and opening avenues for the design of condensates with programmable viscoelastic properties.

  PublisherDOI

• Roadmap for Condensates in Cell Biology

  arXiv (Cornell University) · 2026-01-07

  preprintOpen access

  Biomolecular condensates govern essential cellular processes yet elude description by traditional equilibrium models. This roadmap, distilled from structured discussions at a workshop and reflecting the consensus of its participants, clarifies key concepts for researchers, funding bodies, and journals. After unifying terminology that often separates disciplines, we outline the core physics of condensate formation, review their biological roles, and identify outstanding challenges in nonequilibrium theory, multiscale simulation, and quantitative in-cell measurements. We close with a forward-looking outlook to guide coordinated efforts toward predictive, experimentally anchored understanding and control of biomolecular condensates.

  PublisherDOI

• BPS2026 – A physics-based approach to predict phase behavior of proteins under heat stress

  Biophysical Journal · 2026-02-01

  articleSenior author
  PublisherDOI

• BPS2026 – Development of a multiscale framework for engineering protein condensates as microreactors

  Biophysical Journal · 2026-02-01

  articleSenior author
  PublisherDOI

• BPS2026 – Interplay between mesh reconfigurability and molecular shape memory governs the viscoelasticity of biomolecular condensates

  Biophysical Journal · 2026-02-01

  articleSenior author
  PublisherDOI

• Roadmap for Condensates in Cell Biology

  ArXiv.org · 2026-01-07

  articleOpen access

  Biomolecular condensates govern essential cellular processes yet elude description by traditional equilibrium models. This roadmap, distilled from structured discussions at a workshop and reflecting the consensus of its participants, clarifies key concepts for researchers, funding bodies, and journals. After unifying terminology that often separates disciplines, we outline the core physics of condensate formation, review their biological roles, and identify outstanding challenges in nonequilibrium theory, multiscale simulation, and quantitative in-cell measurements. We close with a forward-looking outlook to guide coordinated efforts toward predictive, experimentally anchored understanding and control of biomolecular condensates.

  PublisherOA PDF

• BPS2026 – Biomolecular condensates dictate the folding landscape of proteins

  Biophysical Journal · 2026-02-01

  articleSenior author
  PublisherDOI

• BPS2026 – What is the structure of biomolecular condensates?

  Biophysical Journal · 2026-02-01

  article
  PublisherDOI

• Biomolecular Condensates Dictate the Folding Landscape of Proteins

  bioRxiv (Cold Spring Harbor Laboratory) · 2026-01-13

  articleOpen accessSenior authorCorresponding

  Protein structure is exquisitely sensitive to the surrounding chemical environment, and many proteins encounter complex environments within cells. Importantly, numerous proteins organize into biomolecular condensates—dense macromolecular assemblies with distinct physicochemical properties. This raises a fundamental question: how does condensation reshape protein structure and dynamics? Here, we investigate how protein folding landscapes are altered inside condensates, using the protein α-helix as a model folded domain. Atomistic simulations show that free energy surfaces within condensates differ markedly from those in dilute solution or in the presence of inert crowders. We then use Bayesian optimization to develop a chemically specific, near-atomistic model for quantification of α-helical folding and apply it to characterize diverse helices, including α-helical domains from the disease-associated proteins TDP43, Annexin A11, and the Androgen Receptor, within condensates of varying physicochemical properties. Our results support a framework in which multivalent interactions drive unfolding while crowding promotes folding, and protein conformational ensembles inside condensates emerge from this balance. Additionally, we show that folding transitions are kinetically frustrated inside condensates because they are coupled to the timescale of contact rearrangement with co-condensate proteins. As such, folding landscapes within condensates are dually sequence-dependent, informed by both the sequence of the folded domain and co-condensate proteins. Together, our work has implications for understanding condensate-mediated proteinopathies, targeting aberrant condensates, and designing condensates to program protein function across scales.

  PublisherDOI

Frequent coauthors

• Rosana Collepardo‐Guevara

  University of Cambridge

  69 shared

• Jorge R. Espinosa

  48 shared

• Maria Julia Maristany

  Marine Biological Laboratory

  26 shared

• J.L. Huertas

  University of Cambridge

  20 shared

• Anne Aguirre Gonzalez

  Universidad Complutense de Madrid

  19 shared

• Adiran Garaizar

  Bayer (Germany)

  16 shared

• Simon Alberti

  TU Dresden

  14 shared

• Tuomas P. J. Knowles

  University of Cambridge

  13 shared

Education

• PhD. Chemistry, Chemistry

  University of Cambridge

  2018

• MPhil. Chemistry, Biological and Chemical Sciences

  University of the West Indies

  2014

• Bsc. Chemistry and Mathematics, Biological and Chemical Sciences

  University of the West Indies

  2012

Awards & honors

• Howard B. Wentz, Jr. Junior Faculty Award, 2026
• Visiting Theorist, Center for Quantitative Living Systems, D…
• Great Teaching Award Letter for CBE 422, School of Engineeri…
• NIGMS MIRA (R35) Award, National Institutes of Health (NIH),…
• Great Teaching Award Letter for CBE 422, School of Engineeri…