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• W2316431065 abstract "We conducted molecular dynamics simulations combined with distance-based umbrella sampling and forward flux sampling to investigate the early stages of protein crystallization. Formation of contacts with long-range interactions and/or an exposed position on the protein surface was kinetically preferred over more stable hydrophobic contacts with a shorter attractive range, while the thermodynamic stability of the protein crystal was provided by hydrophobic interactions. Contacts with a large interaction area showed complex dissociation pathways that were not detected by distance-based umbrella sampling. Instead, forward flux sampling simulations of contact dissociation identified long-range attractive interactions." @default.
• W2316431065 created "2016-06-24" @default.
• W2316431065 creator A5060446256 @default.
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• W2316431065 date "2015-03-30" @default.
• W2316431065 modified "2023-09-25" @default.
• W2316431065 title "Simulation of protein association: Kinetic pathways towards crystal contacts" @default.
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• W2316431065 doi "https://doi.org/10.1103/physreve.91.033311" @default.
• W2316431065 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25871250" @default.
• W2316431065 hasPublicationYear "2015" @default.
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