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Nate

@nathanieldhess.bsky.social

PhD Candidate at Princeton University Chemical and Biological Engineering Department Biomolecular condensates, biophysics, and molecular simulations Member of the Joseph Group (https://josephgroup.princeton.edu/) Princeton '22-Present | Penn '18-'22

23 Followers  |  29 Following  |  4 Posts  |  Joined: 20.01.2025  |  1.6683

Latest posts by nathanieldhess.bsky.social on Bluesky

Many condensates can be described as active soft materials that generate molecular fluxes. Here we develop a new #nonequilibrium approach (TRACE) to study molecular transport through condensates! Work led by Yashraj Wani!!

www.biorxiv.org/content/10.6...

07.02.2026 17:31 β€” πŸ‘ 18    πŸ” 7    πŸ’¬ 1    πŸ“Œ 0

How does protein folding change inside biomolecular condensates?

Our new preprint put forwards a framework for predicting this!! πŸ₯³πŸ₯³πŸ₯³πŸ₯³ work by the talented @nathanieldhess.bsky.social

14.01.2026 21:22 β€” πŸ‘ 35    πŸ” 13    πŸ’¬ 0    πŸ“Œ 0

If you like our article, please also consider reading the great work done by experimental colleagues in the field on this topic, including:

doi.org/10.1073/pnas... from @lek-lab.bsky.social

doi.org/10.1073/pnas... from the Sosnick Group

doi.org/10.1038/s415... from the JD Gross Lab

14.01.2026 21:09 β€” πŸ‘ 1    πŸ” 0    πŸ’¬ 0    πŸ“Œ 0

2. (cont) changes with contact rearrangements to co-condensate proteins.
3. Folding landscapes are dually sequence-dependent, informed by both the folded domain and co-condensate proteins.

(3/4)

14.01.2026 21:09 β€” πŸ‘ 0    πŸ” 0    πŸ’¬ 1    πŸ“Œ 0

Key aspects of our framework include that:

1. Condensates tune protein structure through both multivalent interactions (promotes unfolding) and crowding (promotes folding).
2. Kinetic transitions in protein structures are frustrated within condensates due to coupled conformational

(2/4)

14.01.2026 21:09 β€” πŸ‘ 0    πŸ” 0    πŸ’¬ 1    πŸ“Œ 0
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I am very excited to share our pre-print that was just released on the bioRxiv entitled "Biomolecular Condensates Dictate the Folding Landscape of Proteins" doi.org/10.64898/202...

Very grateful for @jerelleaj.bsky.social and the members of the Joseph Group for their support on this project! (1/4)

14.01.2026 21:09 β€” πŸ‘ 18    πŸ” 5    πŸ’¬ 1    πŸ“Œ 1

Biomolecular Condensates Dictate the Folding Landscape of Proteins https://www.biorxiv.org/content/10.64898/2026.01.12.699095v1

14.01.2026 04:49 β€” πŸ‘ 7    πŸ” 5    πŸ’¬ 0    πŸ“Œ 0
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Now online - the Review "Structured protein domains enter the spotlight: modulators of #biomolecularcondensate form and function" from Nathaniel Hess and @jerelleaj.bsky.social.

#PhaseSeparation #ProteinProteinInteraction #Oligomerization #ProteinRNAInteraction

authors.elsevier.com/sd/article/S...

23.01.2025 15:08 β€” πŸ‘ 27    πŸ” 10    πŸ’¬ 0    πŸ“Œ 0

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