Protein folding and surface interaction phase diagrams in vitro and in cells

Protein stability is subject to environmental perturbations such as pressure and crowding, as well as sticking to other macromolecules and quinary structure. Thus, the environment inside and outside the cell plays a key role in how proteins fold, interact, and function on the scale from a few molecu...

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Bibliographic Details
Published inFEBS letters Vol. 595; no. 9; pp. 1267 - 1274
Main Author Gruebele, Martin
Format Journal Article
LanguageEnglish
Published England 01.05.2021
Subjects
E. coli
homeostasis
Humans
liquids
liquid–liquid phase‐separated regions
Macromolecular Substances - ultrastructure
mammalian cell
Models, Molecular
Protein Folding
Protein Stability
Protein Structure, Quaternary - genetics
Proteins - genetics
Proteins - ultrastructure
quinary structure
separation
protein folding
mammalian cell
liquid-liquid phase-separated regions
E. coli
quinary structure
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Summary:Protein stability is subject to environmental perturbations such as pressure and crowding, as well as sticking to other macromolecules and quinary structure. Thus, the environment inside and outside the cell plays a key role in how proteins fold, interact, and function on the scale from a few molecules to macroscopic ensembles. This review discusses three aspects of protein phase diagrams: first, the relevance of phase diagrams to protein folding and function in vitro and in cells; next, how the evolution of protein surfaces impacts on interaction phase diagrams; and finally, how phase separation plays a role on much larger length‐scales than individual proteins or oligomers, when liquid phase‐separated regions form to assist protein function and cell homeostasis.
Bibliography:Edited by Miguel De la Rosa
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ISSN:0014-5793
1873-3468
1873-3468
DOI:10.1002/1873-3468.14058