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- W3210053954 abstract "Proteins fold into unique three-dimensional structures in aqueous or lipid environments. The conformation of folded proteins is stabilized by non-bonded interactions among main and side chains of polypeptides. In addition to the intramolecular interactions within polypeptide, hydration water molecules confined in the interior of protein have significant contribution to the conformation and stability. Furthermore, proteins form homo- or heterogeneous assemblies and/or molecular associations necessary, for instance, for biological signal transduction. Hydration water molecules function as glue at the protein interfaces to make protein surfaces complementary, and/or as lubricants to assist structural reorganization such as domain motion. In this chapter, we describe the role of hydration water molecules residing inside proteins and at interfaces of their assemblies, and discuss their roles based on high-resolution crystal structures." @default.
- W3210053954 created "2021-11-08" @default.
- W3210053954 creator A5063077785 @default.
- W3210053954 date "2021-01-01" @default.
- W3210053954 modified "2023-09-27" @default.
- W3210053954 title "Hydration Structures Inside Proteins" @default.
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- W3210053954 doi "https://doi.org/10.1007/978-4-431-56919-0_3" @default.
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