Complete Phase Diagram for Liquid-Liquid Phase Separation of Intrinsically Disordered Proteins.

Autor: McCarty J; Department of Chemistry and Biochemistry , University of California , Santa Barbara , California 93106 , United States.; Materials Research Laboratory , University of California , Santa Barbara , California 93106 , United States., Delaney KT; Materials Research Laboratory , University of California , Santa Barbara , California 93106 , United States., Danielsen SPO; Materials Research Laboratory , University of California , Santa Barbara , California 93106 , United States.; Department of Chemical Engineering , University of California , Santa Barbara , California 93106 , United States., Fredrickson GH; Materials Research Laboratory , University of California , Santa Barbara , California 93106 , United States.; Department of Chemical Engineering , University of California , Santa Barbara , California 93106 , United States.; Materials Department , University of California , Santa Barbara , California 93106 , United States., Shea JE; Department of Chemistry and Biochemistry , University of California , Santa Barbara , California 93106 , United States.; Materials Research Laboratory , University of California , Santa Barbara , California 93106 , United States.; Department of Physics , University of California Santa Barbara , Santa Barbara , California 93106 , United States.
Jazyk: angličtina
Zdroj: The journal of physical chemistry letters [J Phys Chem Lett] 2019 Apr 18; Vol. 10 (8), pp. 1644-1652. Date of Electronic Publication: 2019 Mar 27.
DOI: 10.1021/acs.jpclett.9b00099
Abstrakt: A number of intrinsically disordered proteins have been shown to self-assemble via liquid-liquid phase separation into protein-rich and dilute phases. The resulting coacervates can have important biological functions, and the ability to form these assemblies is dictated by the protein's primary amino acid sequence as well as by the solution conditions. We present a complete phase diagram for the simple coacervation of a polyampholyte intrinsically disordered protein using a field-theoretic simulation approach. We show that differences in the primary amino acid sequence and in the distribution of charged amino acids along the sequence lead to differences in the phase window for coacervation, with block-charged sequences having a larger coacervation window than sequences with a random patterning of charges. The model also captures how changing solution conditions modifies the phase diagram and can serve to guide experimental studies.
Databáze: MEDLINE
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