Multi-scale molecular simulation of random peptide phase separation and its extended-to-compact structure transition driven by hydrophobic interactions
- 20 September 2023
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Soft Matter
- Vol. 19 (41) , 7944-7954
Abstract
Stronger hydrophobic interactions result in more compact single-chain structures, elevating the tendency as well as the critical temperature of phase separation.Keywords
Funding Information
- National Natural Science Foundation of China (11947006)
- Hubei University of Medicine (2019QDJZR12, 2020QDJZR015)
- Hubei Provincial Department of Education (2022PHXKQ5)
This publication has 70 references indexed in Scilit:
- A Simple Atomic-Level Hydrophobicity Scale Reveals Protein Interfacial StructureJournal of Molecular Biology, 2014
- Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residuesProceedings of the National Academy of Sciences, 2013
- Predicting phase behavior in multicomponent mixturesThe Journal of Chemical Physics, 2013
- Versatility from Protein DisorderScience, 2012
- Phase transitions in the assembly of multivalent signalling proteinsNature, 2012
- Net charge per residue modulates conformational ensembles of intrinsically disordered proteinsProceedings of the National Academy of Sciences, 2010
- γ-Secretase Heterogeneity in the Aph1 Subunit: Relevance for Alzheimer’s DiseaseScience, 2009
- ABSINTH: A new continuum solvation model for simulations of polypeptides in aqueous solutionsJournal of Computational Chemistry, 2008
- General purpose molecular dynamics simulations fully implemented on graphics processing unitsJournal of Computational Physics, 2008
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982