Biomolecular condensates are membraneless bodies that concentrate biomolecules. Many condensates form via reversible phase transitions and these transitions are driven by multivalent protein and RNA molecules. There is growing interest in the question of how condensates form, how they are regulated, how they dissolve, and how they contribute to cellular functions. The central role of condensates in dysregulation of cellular functions and the development of therapeutics that modulate condensates in bespoke ways is also an area of growing interest. These emerging interests call for a state-of-the-art appraisal of where things stand with respect to key questions regarding the encoding and modulation of the driving forces for condensate formation. In this three lecture series Rohit Pappu will provide an overview of the key physical principles underlying the sequence-to-phase behavior relationships of different archetypes of multivalent protein and RNA molecules. The lectures will largely stay focused on discoveries made individually and jointly by the Pappu lab and key collaborators over the past 3-4 years.

Part 2: Phase transitions of intrinsically disordered proteins. This lecture will adapt the stickers-and-spacers model to explain how different archetypes of IDPs encode different types of phase transitions. The talk will address the issue of how specificity in the driving forces for phase transitions can be gleaned, and potentially prevails even without the consideration of specific structural motifs. This work, which adapts to our thinking about RNA molecules as well, will introduce the importance of different types of stickers and spacers and connect to the prevalence of short linear motifs (SLiMs) as stickers in IDPs. This lecture will also briefly touch upon the importance of concepts from the field of complex coacervation.

Start time in various timezones:
7:00 am PDT
9:00 am CDT
10:00 am EDT
2:00 pm UTC
3:00 pm BST
4:00 pm CET

Note, this is the second talk in a three-part series.
Read more about part one here.
Read more about part three here.

See the video from part one here.
See the video from part two here.
See the video from part three here.

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