ArticleThe journal of physical chemistry. B2021
Thermodynamic Compensation in Peptides Following Liquid-Liquid Phase Separation.
Article in The journal of physical chemistry. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Article
- Amino acid transfer free energies reveal thermodynamic driving forces in biomolecular condensate formation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Amino Acid Transfer Free Energies Reveal Thermodynamic Driving Forces in Biomolecular Condensate Formation.bioRxiv : the preprint server for biology · 2024Article
- Peptide diffusion in biomolecular condensates.Biophysical journal · 2024Article
- Parameter Dependence of the Solubility Limit for Disodium Phosphate.The journal of physical chemistry. B · 2023Article
- Neuronal biomolecular condensates and their implications in neurodegenerative diseases.Frontiers in aging neuroscience · 2023Review
- Effects of Conformational Constraint on Peptide Solubility Limits.The journal of physical chemistry. B · 2022Article
- Multivalent interactions between molecular components involved in fast endophilin mediated endocytosis drive protein phase separation.Nature communications · 2022Article
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Authors and funding
2 authors.
Funding
Abstract
Liquid-liquid phase separation of proteins often incorporates intrinsically disordered proteins or those with disordered regions. Examining these processes via the entropy change is desirable for establishing a quantitative foundation with which to probe and understand these phase transitions. Of interest is the effect of residue sequence on the entropy of the peptide backbone. In this work we model these systems via all atom simulations of liquid-liquid phase separation of peptides. Systems of supersaturated pentapeptides separate into a peptide-dense liquid droplet phase as well as a dilute (saturated) aqueous phase. An analysis of the change in backbone conformational entropy associated with the phase transition was performed. We examined systems of four different pentapeptides (GGGGG, GGQGG, GGNGG, and GGVGG) in order to explore the effect of sequence variation on the conformational entropy, as well as the effect of side chain variation on the physical characteristics of the droplet phases. We find that the loss of conformational entropy that accompanies aqueous → droplet transitions is more than compensated by a decrease in interaction enthalpy as contributions to the free energy change for the process.
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