ArticleProceedings of the National Academy of Sciences of the United States of America2025
The configurational length scale in the self-assembly and modulation of higher-order transient protein structures.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Biomolecular assemblies through weak noncovalent interactions: Higher-order transient structures and their condensate phase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Multispecific nanobody degraders co-deplete membrane receptors and enable targeted delivery of diverse payloads.bioRxiv : the preprint server for biology · 2026Article
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2 authors.
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Abstract
Membrane protein homo-oligomers named higher-order transient structures (HOTS) are formed through cohesive self-interactions in the range of a few [Formula: see text]. The small magnitude of these interactions underlies the rapid reversibility of HOTS on the timescale of membrane signaling processes, permitting the dynamic modulation of signals. At the same time, weak interactions present an apparent paradox: HOTS should form only if the concentration of a particular protein is sufficiently high to produce oligomerization by mass action. And yet, HOTS are observed experimentally with membrane proteins present in cell membranes at concentrations of only a few per [Formula: see text]. In this study, we employ principles of statistical thermodynamics to explain how cells can alter the configurational entropy of the oligomerization reaction, thereby achieving HOTS formation at low concentrations of the protein in the membrane. We propose that this modification of the configurational entropy, a process we call configurational length scaling, is an important aspect of HOTS formation in cell membranes and possibly other cellular compartments.
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