Essential Techniques for Medical and Life Scientists.

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Autor principal: Tutar, Yusuf
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Sharjah : Bentham Science Publishers, 2018.
Temas:
Embedded computer systems > Programming.
Arduino (Programmable controller) > Programming.
Arduino (Automate programmable) > Programmation.
Embedded computer systems > Programming
Acceso en línea:Texto completo
Tabla de Contenidos:
  • Intro; CONTENTS; FOREWORD; PREFACE; List of Contributors; Application of Mass Spectrometry in Proteomics; Serap Pektas*; INTRODUCTION; 1. INLET SYSTEMS; 2. IONIZATION TECHNIQUE; 2.1. Electrospray Ionization (ESI); 2.2. Matrix Assisted Laser Desorption Ionization (MALDI); 2.2.1. MALDI Sample Preparation; 3. MASS ANALYZERS; 3.1. Quadrupole Mass Analyzer; Tandem Mass Spectrometry MS/MS; 3.2. Ion Trap Mass Analyzer (IT); 3.3. Orbitrap Mass Analyzer; 3.4. Time of Flight (TOF) Mass Analyzer; 4. DETECTORS; 5. APPLICATIONS; 5.1. Proteomics; 5.1.1. Molecular Weight Determination.
  • 5.1.2. Protein Sequencing5.1.3. Post-Translational Modifications; 5.1.4. Protein-Protein, Protein-DNA and Protein-Small Molecule Interactions; 5.1.5. Protein Folding and Unfolding Rates; 5.2. Microbiology; 5.3. Medicine; CONSENT FOR PUBLICATION; CONFLICT OF INTEREST; ACKNOWLEDGEMENTS; REFERENCES; Structural Elucidation of Macromolecules; Ana Luísa Carvalho, Teresa Santos-Silva, Maria João Romão, Eurico J. Cabrita and Filipa Marcelo*; INTRODUCTION; 2.1. Solving the 3D Structure of Proteins Using X-ray Crystallography; 2.1.1. Protein Crystallization.
  • 2.1.2. Diffraction of X-rays by Protein Crystals2.1.3. 3D Structure Solution and Refinement; 2.1.4. Validation and Analysis of Crystal Structures; 2.2. NMR Guide into Molecular Recognition; 2.2.1. NMR and the Study of Intermolecular Interactions; 2.2.2. Protein-detected NMR Based Experiments; 2.2.3. Ligand-detected NMR Based Experiments; 2.3. Studying Protein Shape and Protein-ligand Interactions by SAXS Methods; 2.3.1. Data Collection; 2.3.2. Preliminary Sample Characterization: Guinier; Porod, Kratky and Pair Distribution Functions; 2.3.3. Deriving a Structural Model.
  • 2.4. Structural Elucidation Using Cryo-Electron Microscopy2.5. Notes; 2.5.1. Growing and Preserving a Protein Crystal; 2.5.2. Bragg's Law; 2.5.3. Seleno-methionine Derivatives for Structure Solution; 2.5.4. Patterson Maps and Molecular Replacement; 2.5.5. Electron Density Maps; 2.5.5. The Temperature Factor (B Factor); 2.5.6. The Ramachandran Plot; 2.5.7. Technical Aspects of NMR Hardware and Software; 2.5.8. NMR Sample; 2.5.9. General Aspects on Acquisition and Processing of NMR Spectra; 2.5.10. Basics on 15N-1H-HSQC Titrations; 2.5.11. Basics on Transferred NOE.
  • 2.5.12. Basics on STD-NMR Experiments2.5.13. Basics on Diffusion Experiments; 2.5.14. SAXS Buffer Subtraction; 2.5.15. Sample Quality for Successful BioSAXS Experiment; 2.5.16. Radiation Damage; 2.5.17. Small Angle Neutron Scattering (SANS); CONSENT FOR PUBLICATION; CONFLICT OF INTEREST; ACKNOWLEDGEMENTS; REFERENCES; Isothermal Titration Calorimetry; Ozlem Ustun Aytekin1, Elvan Yilmaz Akyuz1, Banu Bayram1, Esen Tutar2, Halime Hanım Pence3 and Yusuf Tutar1,4,*; INTRODUCTION; 3.1. ITC in Protein Science and Enzyme Technology; 3.1.1. Protein-protein Interactions.

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