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Biomolecules. 2019 Dec 8;9(12). pii: E842. doi: 10.3390/biom9120842.

Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions.

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Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.
Laboratory of New Methods in Biology, Institute for Biological Instrumentation, Russian Academy of Sciences, Federal Research Center "Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences", 142290 Pushchino, Moscow, Russia.
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow, Russia.
Biology Department, Lomonosov Moscow State University, 119192 Moscow, Russia.
Bioltechnogy Department, Lomonosov Moscow State University, 142290 Pushchino, Moscow, Russia.


Proteins, these evolutionarily-edited biological polymers, are able to undergo intramolecular and intermolecular phase transitions. Spontaneous intramolecular phase transitions define the folding of globular proteins, whereas binding-induced, intra- and inter- molecular phase transitions play a crucial role in the functionality of many intrinsically-disordered proteins. On the other hand, intermolecular phase transitions are the behind-the-scenes players in a diverse set of macrosystemic phenomena taking place in protein solutions, such as new phase nucleation in bulk, on the interface, and on the impurities, protein crystallization, protein aggregation, the formation of amyloid fibrils, and intermolecular liquid-liquid or liquid-gel phase transitions associated with the biogenesis of membraneless organelles in the cells. This review is dedicated to the systematic analysis of the phase behavior of protein molecules and their ensembles, and provides a description of the major physical principles governing intramolecular and intermolecular phase transitions in protein solutions.


amyloid fibril; coil; crystal; intrinsically-disordered protein; liquid–liquid phase separation; membraneless organelle; molten globule; phase transition; protein folding; protein structure; secondary structure

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