Molecular Structures and Structural Dynamics of Prion Proteins and Prions (eBook)
XIX, 355 Seiten
Springer Netherland (Verlag)
978-94-017-7318-8 (ISBN)
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.
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 "e;protein structural conformational"e; diseases.PrPC is predominant in a-helices but PrPSc are rich in -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.
1. Basic KnowledgePart I Molecular Dynamics of Prion Proteins2. The Homology Structure and Dynamics3. The NMR Structure and Dynamics of the Wild-type and Mutants4. Compared with the NMR Structure and Dynamics of Humans and Mice5. Compared with the NMR Structure and Dynamics of Dogs and Horses6. Compared with a Homology Structure and Dynamics of Buffaloes7. Compared with NMR Structure and Dynamics of Elks 8. Compared with the X-ray Structure and Dynamics of Rabbits 9. Surface Electrostatic Charge Distributions 10. The Hydrophobic Region PrP(109–136) Part II Molecular Modeling of Prions11. The Hybrid Method of Steepest Descent - Conjugate Gradient with Simulated Annealing 12. Hybrid Method of Discrete Gradient with Simulated Annealing or Genetic Algorithm 13. A Novel Canonical Dual Global Optimization Computational Approach 14. The Hybrid Method of Evolutionary Computations with Simulated Annealing15. Simulated Annealing Refined Replica Exchange Global Search Algorithm16. LBFGS Quasi-Newtonian Methods for MM Prion AGAAAAGA Amyloid Fibrils17. Particle Swarm Global Optimization Search Algorithm18. A Summary of the Research Works on AGAAAAGAReferencesIndex
Erscheint lt. Verlag | 14.9.2015 |
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Reihe/Serie | Focus on Structural Biology | Focus on Structural Biology |
Zusatzinfo | XIX, 355 p. 179 illus., 176 illus. in color. |
Verlagsort | Dordrecht |
Sprache | englisch |
Themenwelt | Mathematik / Informatik ► Informatik |
Medizin / Pharmazie | |
Naturwissenschaften ► Biologie ► Biochemie | |
Naturwissenschaften ► Biologie ► Mikrobiologie / Immunologie | |
Naturwissenschaften ► Chemie ► Physikalische Chemie | |
Naturwissenschaften ► Physik / Astronomie ► Angewandte Physik | |
Technik | |
Schlagworte | Molecular Modeling • Molecular Structures • Prion Amyloid Fibrils • prion diseases • Prion Proteins • Protein Structure |
ISBN-10 | 94-017-7318-1 / 9401773181 |
ISBN-13 | 978-94-017-7318-8 / 9789401773188 |
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