rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Molecular Dynamics Analyses of Prion Protein Structures
    sub title: The Resistance to Prion Diseases Down Under
  name:
    name part: Zhang, Jiapu.
    role:
      role term: creator
    role:
      role term: author.
    role:
      role term: aut
    role:
      role term: http://id.loc.gov/vocabulary/relators/aut
  name:
    name part: SpringerLink (Online service)
  type of resource: text
  origin info:
    place:
      place term: si
    date issued: 2018
    edition: 1st ed. 2018.
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: electronic
    form: electronic resource
    reformatting quality: access
    form: remote
    extent: XXIX, 375 p. 596 illus., 278 illus. in color. online resource.
  abstract: Unlike 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 β2-α2 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-β 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.
  table of contents: Preface -- 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. .
  note: by Jiapu Zhang.
  subject:
    topic: Proteomics
  subject:
    topic: Proteomics
  classification: QD431-431.7
  classification: 572.6
  related item:
    title info:
      title: Springer eBooks
  related item:
    title info:
      title: Focus on Structural Biology, 10
  identifier: 9789811088155
  identifier: https://doi.org/10.1007/978-981-10-8815-5
  record info:
    record creation date: 180720
    record change date: 20190620092103.0
    record identifier: 978-981-10-8815-5