Document Type

Article

Publication Date

2019

Keywords

Protein Folding, Protein Structure, Intrinsically-disordered Protein, Molten Globule, Secondary Structure, Coil, Phase Transition, Liquid–liquid Phase Separation, Membraneless Organelle, Amyloid Fibril, Crystal

Digital Object Identifier (DOI)

https://www.mdpi.com/2218-273X/9/12/842#

Abstract

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.

Rights Information

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Biomolecules, v. 9, issue 12, art. 842

Share

COinS