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Updated: Jul 4, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Biomolecular assemblies through weak noncovalent interactions: Higher-order transient structures and their condensate
Roderick MacKinnon1, Christoph A Haselwandter2,3
1Laboratory of Molecular Neurobiology and Biophysics, HHMI, The Rockefeller University, New York, NY 10065.
Abstract:
Recent data suggest that many membrane proteins spontaneously organize into spatial patterns through weak noncovalent interactions. These weak interactions are protein type-specific and underlie the formation of higher-order transient structures (HOTS), which can function as 10 to 100 nanometer-sized, transient hubs of membrane signaling. We describe the necessary conditions for HOTS assembly to occur, its thermodynamic relationship to biomolecular condensate formation, and potential roles of HOTS in biology stemming from their unique physical properties. Currently, a quantitative understanding of HOTS is limited to membrane proteins, but many observations suggest that HOTS may also be abundant in three-dimensional cellular compartments.
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