Protein aggregation/crystallization and minor structural changes: universal vs specific aspects

Antonio Emanuele, Filippo Pullara

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


Protein association covers wide interests in biophysics, protein science, and biotechnologies, and it is often viewed as governed by conformation details. More recently, the existence of a universal physical principle governing aggregation/crystallization processes has been suggested by a series of experiments and shown to be linked to the universal scaling properties of concentration fluctuations occurring in the proximity of a phase transition (spinodal demixing in the specific case). Suchproperties have provided a quantitative basis for capturing kinetic association data on a universal master curve, ruled by the normalized distance of the state of the system from its instability region. Here we report new data on lysozyme crystal nucleation. They strengthen the evidence in favor of universality and show that the system enters the region of universal behavior in a stepwise manner as a result of minor conformation changes. Results also show that the link between conformation details and universal behavior is actuated by interactions mediated by the solvent. Outside the region of universal behavior, nucleation rates become unpredictable and undetectably long.
Original languageEnglish
Pages (from-to)3271-3278
JournalBiophysical Journal
Publication statusPublished - 2007

All Science Journal Classification (ASJC) codes

  • Biophysics

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