Author

Rashik Ahmed

University of TorontoORCID 0000-0003-2001-9684Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:protein structure· 3 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:protein sequence· 1 Approach:statistical model· 1

Frequent Co-Authors

Julie Deborah Forman-KayiD· 3 shared Lewis E. KayiD· 2 shared Rhea P. HudsoniD· 2 shared A. K. RangaduraiiD· 1 shared Bernd BukauiD· 1 shared Jeffrey P. BoniniD· 1 shared Lewis E. KayiD· 1 shared Lucia SvobodaiD· 1 shared

Activity by Year

2024-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersBiophysics

Julie Deborah Forman-KayORCID

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3 papers

Recent·Most cited

Phase separation reshapes the conformational energy landscape of a chaperone to prime its activity

Rashik Ahmed, Lucia Svoboda, Rhea P Hudson, Jeffrey P. Bonin, Bernd Bukau, Julie Deborah Forman-Kay, Lewis E. Kay

This study shows how phase separation alters the conformational dynamics of DNAJB1, priming it for HSP70 binding and stress granule disassembly.

bioRxiv · Oct 22, 2026 · PreprintBiophysics

Client-scaffold interactions suppress aggregation of a client protein in model condensates

Rashik Ahmed, Rhea P. Hudson, Julie Deborah Forman-Kay, Lewis E. Kay

This paper shows that CAPRIN1 condensates suppress FUS RRM aggregation despite increasing its concentration and unfolding it, by outcompeting homotypic intermolecular contacts.

Proceedings of the National Academy of Sciences · Aug 12, 2025Peer-reviewedBiophysics

Atomic resolution map of the solvent interactions driving SOD1 unfolding in CAPRIN1 condensates

Rashik Ahmed, Mingyang Liang, Rhea P. Hudson, A. K. Rangadurai, Shuya Kate Huang, Julie Deborah Forman-Kay, Lewis E. Kay

This study uses NMR to show CAPRIN1 condensates shift SOD1 folding towards unfolded states, promoting aggregation, while a zinc-bound dimeric form is more stable.

Proceedings of the National Academy of Sciences · Aug 22, 2024Peer-reviewedBiophysics