Protein shape modulates crowding effects

Protein shape modulates crowding effects

Protein−protein interactions are usually studied in dilute buffered solutions with macromolecule concentrations of

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Bibliographische Detailangaben
Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 2018-10, Vol.115 (43), p.10965-10970
Hauptverfasser: Guseman, Alex J., Goncalves, Gerardo M. Perez, Speer, Shannon L., Young, Gregory B., Pielak, Gary J.
Format: Artikel
Sprache:eng
Schlagworte:
Biological Sciences
Chemical interactions
Crowding
Dimers
Ficoll - chemistry
Homeostasis
Macromolecular Substances - chemistry
Macromolecules
Mutagenesis
Mutation
Organic chemistry
Particle theory
Physical Sciences
Polyethylene glycol
Polyethylene Glycols - chemistry
Polymers - chemistry
Protein G
Protein interaction
Protein Interaction Maps - physiology
Protein Multimerization - physiology
Proteins
Proteins - chemistry
Shape effects
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Beschreibung
Zusammenfassung:Protein−protein interactions are usually studied in dilute buffered solutions with macromolecule concentrations of
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1810054115