01631oam 2200457zu 450 99620208860331620210807002720.01-5090-8803-2(CKB)1000000000331036(SSID)ssj0000393754(PQKBManifestationID)12123060(PQKBTitleCode)TC0000393754(PQKBWorkID)10378495(PQKB)11447917(EXLCZ)99100000000033103620160829d2007 uy engtxtccrSeventh International Symposium on Cluster Computing and the Grid : CCGrid 2007 : 14-17 May, 2007, Rio de Janerio, Brazil[Place of publication not identified]IEEE2007Bibliographic Level Mode of Issuance: Monograph0-7695-2833-3 Computational grids (Computer systems)CongressesHigh performance computingCongressesEngineering & Applied SciencesHILCCComputer ScienceHILCCComputational grids (Computer systems)High performance computingEngineering & Applied SciencesComputer Science004/.36Schulze BrunoIEEE Computer SocietyIEEE International Symposium on Cluster Computing and the GridPQKBPROCEEDING996202088603316Seventh International Symposium on Cluster Computing and the Grid : CCGrid 2007 : 14-17 May, 2007, Rio de Janerio, Brazil2304309UNISA05969nam 22007815 450 991029826730332120200630135227.094-017-7318-110.1007/978-94-017-7318-8(CKB)3710000000477121(EBL)4179193(SSID)ssj0001583855(PQKBManifestationID)16263691(PQKBTitleCode)TC0001583855(PQKBWorkID)14864258(PQKB)10780611(DE-He213)978-94-017-7318-8(MiAaPQ)EBC4179193(PPN)190533544(EXLCZ)99371000000047712120150914d2015 u| 0engur|n|---|||||txtccrMolecular Structures and Structural Dynamics of Prion Proteins and Prions Mechanism Underlying the Resistance to Prion Diseases /by Jiapu Zhang1st ed. 2015.Dordrecht :Springer Netherlands :Imprint: Springer,2015.1 online resource (366 p.)Focus on Structural Biology,1571-4853 ;9Description based upon print version of record.94-017-7317-3 Includes bibliographical references and index.Basic Knowledge -- The Homology Structure and Dynamics -- The NMR Structure and Dynamics of the Wild-type and Mutants -- Compared with the NMR Structure and Dynamics of Humans and Mice -- Compared with the NMR Structure and Dynamics of Dogs and Horses -- Compared with a Homology Structure and Dynamics of Buffaloes -- Compared with NMR Structure and Dynamics of Elks -- Compared with the X-ray Structure and Dynamics of Rabbits -- Surface Electrostatic Charge Distributions -- The Hydrophobic Region PrP(109–136) -- The Hybrid Method of Steepest Descent - Conjugate Gradient with Simulated Annealing -- Hybrid Method of Discrete Gradient with Simulated Annealing or Genetic Algorithm -- A Novel Canonical Dual Global Optimization Computational Approach -- The Hybrid Method of Evolutionary Computations with Simulated Annealing -- Simulated Annealing Refined Replica Exchange Global Search Algorithm -- LBFGS Quasi-Newtonian Methods for MM Prion AGAAAAGA Amyloid Fibrils -- Particle Swarm Global Optimization Search Algorithm -- A Summary of the Research Works on AGAAAAGA.This monograph is the first easy-to-read-and-understand book on prion proteins' molecular dynamics (MD) simulations and on prions' molecular modelling (MM) constructions.  It enables researchers to see what is crucial to the conformational change from normal cellular prion protein (PrPC) to diseased infectious prions (PrPSc), using MD and MM techniques. As we all know, prion diseases, caused by the body's own proteins, are invariably fatal and highly infectious neurodegenerative diseases effecting humans and almost all animals for a major public health concern. Prion contains no nucleic acids and it is a misshapen or conformation-changed protein that acts like an infectious agent; thus prion diseases are called “protein structural conformational” diseases. PrPC is predominant in α-helices but PrPSc are rich in β-sheets in the form as amyloid fibrils; so very amenable to be studied by MD techniques. Through MD, studies on the protein structures and the structural conversion are very important for revealing secrets of prion diseases and for structure-based drug design or discovery. Rabbits, dogs, horses and buffaloes are reported to be the few low susceptibility species to prion diseases; this book's MD studies on these species are clearly helpful to understand the mechanism underlying the resistance to prion diseases. PrP(1-120) usually has no clear molecular structures; this book also studies this unstructured region through MD and especially MM techniques from the global optimization point of view. This book is ideal for practitioners in computing of biophysics, biochemistry, biomedicine, bioinformatics, cheminformatics, materials science and engineering, 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.Focus on Structural Biology,1571-4853 ;9Proteins Molecular biologyBioinformaticsChemistry, Physical and theoreticalBiophysicsBiological physicsProtein Structurehttps://scigraph.springernature.com/ontologies/product-market-codes/L14050Molecular Medicinehttps://scigraph.springernature.com/ontologies/product-market-codes/B1700XComputational Biology/Bioinformaticshttps://scigraph.springernature.com/ontologies/product-market-codes/I23050Theoretical and Computational Chemistryhttps://scigraph.springernature.com/ontologies/product-market-codes/C25007Biological and Medical Physics, Biophysicshttps://scigraph.springernature.com/ontologies/product-market-codes/P27008Proteins .Molecular biology.Bioinformatics.Chemistry, Physical and theoretical.Biophysics.Biological physics.Protein Structure.Molecular Medicine.Computational Biology/Bioinformatics.Theoretical and Computational Chemistry.Biological and Medical Physics, Biophysics.616.83Zhang Jiapuauthttp://id.loc.gov/vocabulary/relators/aut768810MiAaPQMiAaPQMiAaPQBOOK9910298267303321Molecular Structures and Structural Dynamics of Prion Proteins and Prions2541191UNINA