LEADER 03455nam 22005895 450 001 9910731477003321 005 20230803193649.0 010 $a3-031-31871-4 024 7 $a10.1007/978-3-031-31871-9 035 $a(MiAaPQ)EBC30592737 035 $a(Au-PeEL)EBL30592737 035 $a(DE-He213)978-3-031-31871-9 035 $a(PPN)272263877 035 $a(CKB)26938272900041 035 $a(EXLCZ)9926938272900041 100 $a20230612d2023 u| 0 101 0 $aeng 135 $aurcnu|||||||| 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aSolvent-Induced Interactions and Forces in Protein Folding $eHydrophobic-Hydrophilic Phenomena /$fby Arieh Ben-Naim 205 $a1st ed. 2023. 210 1$aCham :$cSpringer Nature Switzerland :$cImprint: Springer,$d2023. 215 $a1 online resource (185 pages) 225 1 $aPhysical Chemistry in Action,$x2197-4357 311 08$aPrint version: Ben-Naim, Arieh Solvent-Induced Interactions and Forces in Protein Folding Cham : Springer,c2023 9783031318702 327 $aIntroduction, definitions and motivations for studying solvent-induced interactions -- A Brief Introduction to Statistical Thermodynamics -- Solvent-induced interactions and forces, definitions and connections with thermodynamics -- Hydrophobic interactions and forces -- Hydrophilic Interactions and Forces -- Implementation of the H?I interactions and forces in some biochemical processes -- Appendix A. The BN3D model of water and the corresponding pair potential -- Appendix B. Solvation thermodynamics of water in liquid water. . 330 $aThis monograph presents the molecular theory and necessary tools for the study of solvent-induced interactions and forces. After introducing the reader to the basic definitions of solvent-induced interactions, the author provides a brief analysis of the statistical thermodynamics. The book thoroughly overviews the connection of those interactions with thermodynamics and consequently focuses on specifically discussing the hydrophobic-hydrophilic interactions and forces. The importance of the implementation of hydrophilic interactions and forces in various biochemical processes is thoroughly analyzed, while evidence based on theory, experiments, and simulated calculations supporting that hydrophilic interactions and forces are far more important than the corresponding hydrophobic effects in many biochemical processes such as protein folding, self-assembly of proteins, molecular recognitions, are described in detail. This title is of great interest to students and researchers working in the fields of chemistry, physics, biochemistry, and molecular biology. 410 0$aPhysical Chemistry in Action,$x2197-4357 606 $aThermodynamics 606 $aPhysical biochemistry 606 $aProteins 606 $aThermodynamics 606 $aBiophysical Chemistry 606 $aProteins 615 0$aThermodynamics. 615 0$aPhysical biochemistry. 615 0$aProteins. 615 14$aThermodynamics. 615 24$aBiophysical Chemistry. 615 24$aProteins. 676 $a541.3482 676 $a541.3482 700 $aBen-Naim$b Arieh$0471923 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910731477003321 996 $aSolvent-Induced Interactions and Forces in Protein Folding$93394861 997 $aUNINA