LEADER 04125nam 22004335 450 001 9910298603503321 005 20200706101448.0 010 $a981-10-8815-2 024 7 $a10.1007/978-981-10-8815-5 035 $a(CKB)4100000005323407 035 $a(DE-He213)978-981-10-8815-5 035 $a(MiAaPQ)EBC5471992 035 $a(PPN)22949952X 035 $a(EXLCZ)994100000005323407 100 $a20180720d2018 u| 0 101 0 $aeng 135 $aurnn|008mamaa 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aMolecular Dynamics Analyses of Prion Protein Structures $eThe Resistance to Prion Diseases Down Under /$fby Jiapu Zhang 205 $a1st ed. 2018. 210 1$aSingapore :$cSpringer Singapore :$cImprint: Springer,$d2018. 215 $a1 online resource (XXIX, 375 p. 596 illus., 278 illus. in color.) 225 1 $aFocus on Structural Biology,$x1571-4853 ;$v10 311 $a981-10-8814-4 327 $aPreface -- Basic Knowledge -- Part I Prion Resistance Species -- Rabbits -Wild-type and Mutants -- Dogs -Wild-type and D159NMutant -- Horses, Buffaloes, and Pigs -- Chicken, Turtles, and Frogs -- Other Species -- Part II b 2-a2 Loop -- Wild-type Mouse 37 oC and 19.85 oC Structures -- Mouse Mutants -- Other Species with an Ordered b 2-a2 -- Part III Human Mutants -- Human Mutants -- Human PrPC Monomer, Dimer and Its M129V Mutant -- Human Peptides -- Part IV PrP Binding/Docking -- PrP Bounded to Antibodies, Nanobody, RNA aptamer, etc -- Potential Antiprion Drugs -- Part V Prion Peptides with Cross-b Structures -- Mathematical Formulas for All PrP Peptides? cross-b structures -- Hydrogen Bonds Between Two Optimized Fundamental Chains of Each Model -- References. . 330 $aUnlike bacteria and viruses, which are based on DNA and RNA, prions are unique as disease-causing agents since they are misfolded proteins. Prion diseases are called "protein structural conformational? diseases. This monograph is the book on molecular dynamics (MD) simulations nearly for all the known normal prion protein (PrPC) PDB entries in the Protein Data Bank (PDB) and associations. Pig is a species that is largely resistant to prions, and chicken, turtles, frogs are species resisting prion infection too; firstly, this book will address all PrP strong immunity species (such as rabbits, dogs, horses, water buffaloes, pigs, chicken, turtles, frogs), compared with high susceptibility species. Other PrP models and doppel models are also MD studied in this book. Secondly, all the mutants of mouse PrP and human PrP are well studied by this book. Mouse mutations in the ?2-?2 loop and the C-terminal will bring clear structures with highly and clearly ordered loop structures. Human mutations will cause prion diseases such as Creutzfeldt-Jakob diseases (CJDs), Gerstmann-Sträussler-Scheinker (GSS) syndrome, fatal familial insomnia (FFI), etc. Deep MD analyses of mouse and human mutants are done in this book. Thirdly, PrP binding with antibodies/compounds etc. is well MD studied in this book. The informatics of potential antiprion drugs known will be revealed. Lastly, cross-? structure PrP peptides are well studied. This book is ideal for practical computing staff in the fields of computational physics, computational biology, computational chemistry, biomedicine, bioinformatics, cheminformatics, materials, applied mathematics and theoretical physics, information technology, operations research, biostatistics, etc. As an accessible introduction to these fields, this book is also ideal as a teaching material for students. 410 0$aFocus on Structural Biology,$x1571-4853 ;$v10 606 $aProteomics 606 $aProteomics$3https://scigraph.springernature.com/ontologies/product-market-codes/L1403X 615 0$aProteomics. 615 14$aProteomics. 676 $a572.6 700 $aZhang$b Jiapu$4aut$4http://id.loc.gov/vocabulary/relators/aut$0768810 906 $aBOOK 912 $a9910298603503321 996 $aMolecular Dynamics Analyses of Prion Protein Structures$91566700 997 $aUNINA