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4D Imaging of Protein Aggregation in Live Cells
Published on: April 5, 2013
Protein aggregation/crystallization and minor structural changes: universal versus specific aspects
F Pullara1, A Emanuele, M B Palma-Vittorelli
1Department of Physical and Astronomical Sciences, University of Palermo, I-90123, Palermo, Italy.
Biophysical Journal
|July 31, 2007
Summary
Protein aggregation and crystallization follow a universal physical principle linked to phase transitions. Lysozyme crystal nucleation data confirm this universality, showing stepwise entry into universal behavior driven by solvent-mediated interactions.
Area of Science:
- Biophysics
- Protein Science
- Biotechnology
- Crystallization
Background:
- Protein association is crucial in biophysics and biotechnology, often linked to conformational changes.
- Recent studies suggest a universal physical principle governs protein aggregation and crystallization, related to phase transitions and concentration fluctuations.
- This principle provides a quantitative framework for understanding kinetic association data via a universal master curve.
Purpose of the Study:
- To investigate lysozyme crystal nucleation to strengthen evidence for a universal physical principle governing protein aggregation.
- To elucidate the relationship between conformational changes, solvent-mediated interactions, and universal behavior in protein crystallization.
Main Methods:
- Experimental analysis of lysozyme crystal nucleation rates.
- Quantitative assessment of concentration fluctuations near a phase transition (spinodal demixing).
- Characterization of system behavior relative to its instability region.
Main Results:
- New data on lysozyme crystal nucleation provide strong support for the universality of protein aggregation/crystallization.
- The system transitions into a region of universal behavior stepwise, influenced by minor conformational alterations.
- Solvent-mediated interactions are identified as the key mechanism linking conformational details to universal behavior.
Conclusions:
- The findings reinforce the existence of a universal physical principle governing protein association, applicable to crystallization processes.
- Understanding the stepwise entry into universal behavior offers new insights into controlling protein crystallization.
- Deviations from universal behavior lead to unpredictable and extremely slow nucleation rates.
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