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• W2031833947 abstract "Water is an integral part of protein complexes. It shapes protein binding sites by filling cavities and it bridges local contacts by hydrogen bonds. However, water molecules are usually not included in protein interface models in the past, and few distribution profiles of water molecules in protein binding interfaces are known. In this work, we use a tripartite protein-water-protein interface model and a nested-ring atom re-organization method to detect hydration trends and patterns from an interface data set which involves immobilized interfacial water molecules. This data set consists of 206 obligate interfaces, 160 non-obligate interfaces, and 522 crystal packing contacts. The two types of biological interfaces are found to be drier than the crystal packing interfaces in our data, agreeable to a hydration pattern reported earlier although the previous definition of immobilized water is pure distance-based. The biological interfaces in our data set are also found to be subject to stronger water exclusion in their formation. To study the overall hydration trend in protein binding interfaces, atoms at the same burial level in each tripartite protein-water-protein interface are organized into a ring. The rings of an interface are then ordered with the core atoms placed at the middle of the structure to form a nested-ring topology. We find that water molecules on the rings of an interface are generally configured in a dry-core-wet-rim pattern with a progressive level-wise solvation towards to the rim of the interface. This solvation trend becomes even sharper when counterexamples are separated. Immobilized water molecules are regularly organized in protein binding interfaces and they should be carefully considered in the studies of protein hydration mechanisms." @default.
• W2031833947 created "2016-06-24" @default.
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• W2031833947 date "2012-03-27" @default.
• W2031833947 modified "2023-10-10" @default.
• W2031833947 title "Progressive dry-core-wet-rim hydration trend in a nested-ring topology of protein binding interfaces" @default.
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• W2031833947 doi "https://doi.org/10.1186/1471-2105-13-51" @default.
• W2031833947 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3373366" @default.
• W2031833947 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22452998" @default.
• W2031833947 hasPublicationYear "2012" @default.
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