Biochemistry Seminar: Benjamin Schuster, "Negative noodles, and positive ones too: Biophysics and bioengineering of intrinsically disordered proteins"

Dates
Wed, Apr 30, 2025 - 12:00 PM 鈥 Wed, Apr 30, 2025 - 01:00 PM
Admission Fee
Free. Refreshments will be available in the ASRC Cafe at 11:30 AM.
Event Address
This speaker will be in-person at the ASRC Main Auditorium, 85 Saint Nicholas Terrace.
Phone Number
212-650-8803
Secondary Phone
212-650-8803
Event Location
This seminar will also be available by Zoom. Zoom link: https://gc-cuny.zoom.us/j/91649779930?pwd=97wFVB14nZr0BasIrb8M6afmDRhbBM.1 Meeting ID: 916 4977 9930. Passcode: ASRC/CCNY. Full names must be used to be admitted.
Event Details

Benjamin Schuster, Assistant Professor, Department of Chemical and Biochemical Engineering, Rutgers University, New Brunswick, NJ, will give a talk titled, "Negative noodles, and positive ones too: Biophysics and bioengineering of intrinsically disordered proteins."

This seminar will also be available by Zoom. Zoom link: ; Meeting ID: 916 4977 9930.  Passcode:  ASRC/CCNY

Please note

* Full names must be used to be admitted to the Zoom meeting.

* The Zoom meeting will be closed and locked at 12:15 p.m., and no one will be able to enter the meeting after that time.

 

ABSTRACT

Intrinsically disordered proteins (IDPs) do not fold into a fixed three-dimensional structure, yet they play important roles in biology. For instance, many IDPs phase separate into biomolecular condensates that function as membrane-less organelles in cells. If IDPs are somewhat like a cooked noodle, then condensates are roughly akin to a ball of cooked spaghetti, or perhaps pasta primavera. In this talk, I will describe three recent studies from my lab and collaborators, relating to the biophysics and bioengineering of these 鈥渘oodles.鈥 I will begin by discussing engineered IDPs (including highly charged sequences) that have provided new insights into the molecular grammar of protein phase separation. Second, I will present biophysical insights into the role of protein condensation in the SARS-CoV-2 viral lifecycle, focusing on how phosphorylation within a cationic disordered region toggles the material state and function of nucleocapsid protein condensates. Third, I will demonstrate how nanoparticle surface engineering allowed us to achieve controlled and orthogonal partitioning of large particles into IDP condensates. Together, these vignettes help link IDP sequence, phase behavior, rheology, and function, with implications for condensate biology and therapeutic targeting of condensates in disease.

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