John Straub
Boston University, MA·Biophysics
Inside cells, some proteins gather into liquid droplets, much like oil separating from water. This process, called liquid-liquid phase separation (LLPS), helps organize normal cell activities.
- Fields
Biophysics
Chemistry
Physics
- Topics
liquid-liquid phase separation
biomolecular condensates
intrinsically disordered proteins
- Grants
- 1 known grant, through Jun 2027
What they work on
- Identify factors that govern liquid-liquid phase separation and later amyloid aggregation of the disordered proteins tau and alpha-synuclein, combining experiments with computer simulations.
- Model tau and alpha-synuclein shapes and hydration-water motion inside protein droplets using multiscale simulations that combine molecular dynamics with field theory.
- Map the phase behavior of tau and alpha-synuclein, comparing simulation predictions with EPR, Overhauser dynamic nuclear polarization and neutron scattering data from partner labs.
More about the research
Under some conditions, however, the droplets may help proteins clump into amyloid fibrils, the sticky fibers found in neurodegenerative diseases. Little is known about the basic properties of these droplets or how they can promote harmful clumping.
Why it matters
Tau and alpha-synuclein form aggregates in neurodegenerative diseases. By revealing how protein droplets can become a route to harmful clumping, this basic research could clarify the molecular origins of protein aggregation diseases. It could eventually inform efforts to understand and intervene in these disorders.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
John Franck
Syracuse University, NY·Chemistry·Early-career
Build instrumentation and open-source analysis software that turn liquid-state Overhauser Dynamic Nuclear Polarization (ODNP) into a routine method for characterizing hydration water around macromolecules.
David Eliezer
Weill Medical College of Cornell University, NY·Biophysics
Determine the structure of a membrane-induced toxic tau oligomer, a small clump of the Alzheimer's-linked protein tau that forms on membranes, using solid-state NMR and ESR spectroscopy.
Atul Parikh
University of California-Davis, CA·Biophysics
Quantify how liquid droplets coarsen, growing and merging over time, during liquid-liquid phase separation confined inside giant vesicles, using fluorescence microscopy and quantitative image analysis.
The school
Boston University: 26 labs on PI Pages, $784M a year on research, 630 research doctorates a year.
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