NMR in Medicine and Biology (häftad)
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Format
Häftad (Paperback / softback)
Språk
Engelska
Antal sidor
217
Utgivningsdatum
2012-02-24
Upplaga
Softcover reprint of the original 1st ed. 1991
Förlag
Springer-Verlag Berlin and Heidelberg GmbH & Co. K
Medarbetare
Kalbitzer, Hans R.
Illustrationer
13 Tables, black and white; XVI, 217 p.
Dimensioner
234 x 156 x 13 mm
Vikt
336 g
Antal komponenter
1
Komponenter
1 Paperback / softback
ISBN
9783642761065
NMR in Medicine and Biology (häftad)

NMR in Medicine and Biology

Structure Determination, Tomography, In Vivo Spectroscopy

Häftad Engelska, 2012-02-24
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0 e From the reviews of the German edition: "NMR: readable yet professional... Through this book the reader with a scientific background becomes familiar with all important NMR phenomena, methods and conceptions... The great amount of carefully drawn figures and skillfully selected biologically relevant spectra and figures are an decisive bridge to the ... aim, to convey the NMR basics without mathematics. Besides biologists and physicians the book can be highly recommended to physicists and chemists..." #Nachrichten a. d. Chemie, Technik u. Laboratorien#1 "An extraordinary NMR textbook ... The authors succeeded in presenting the subject vividly. This book is clearly set out and easy to follow at a glance, and its numerous figures are extremely well done." #Labo#2
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From the reviews of the German edition: "NMR: readable yet professional... Through this book the reader with a scientific background becomes familiar with all important NMR phenomena, methods and conceptions... The great amount of carefully drawn figures and skillfully selected biologically relevant spectra and figures are an decisive bridge to the ... aim, to convey the NMR basics without mathematics. Besides biologists and physicians the book can be highly recommended to physicists and chemists..." #Nachrichten a. d. Chemie, Technik u. Laboratorien#1 "An extraordinary NMR textbook ... The authors succeeded in presenting the subject vividly. This book is clearly set out and easy to follow at a glance, and its numerous figures are extremely well done." #Labo#2

Innehållsförteckning

1. Principles of NMR.- 1.1 The Basic Principle of Magnetic Resonance.- 1.1.1 Magnetic Moment and Nuclear Spin.- 1.1.2 Resonance Condition.- 1.1.3 Bloch Equations.- 1.1.4 Spin-Lattice Relaxation.- 1.1.5 Decay of the Transverse Magnetization and Spin-Spin Relaxation.- 1.2 The NMR Spectrum.- 1.2.1 Chemical Shift.- 1.2.2 Dipole-Dipole Coupling.- 1.2.3 Indirect Spin-Spin Coupling.- 1.2.4 Nucleus-Electron Interaction.- 1.2.5 Nuclear Quadrupole Interaction.- 1.3 Relaxation Mechanisms.- 1.3.1 Transverse Relaxation and Line Width.- 1.3.2 Time-Dependence of Interactions.- 1.3.3 Dipolar Relaxation.- 1.3.4 Relaxation by Chemical Shift Anisotropy.- 1.3.5 Relaxation by Indirect Spin-Spin Coupling.- 1.3.6 Quadrupolar Relaxation.- 1.3.7 Paramagnetic Relaxation.- 1.4 Experimental Methods.- 1.4.1 Continuous-Wave Detection of NMR.- 1.4.2 Pulsed NMR.- 1.4.3 The NMR Spectrometer.- 2. NMR Spectroscopy in Biochemistry.- 2.1 NMR as Analytical Method.- 2.1.1 Identification of Known and Unknown Substances.- 2.1.2 The Internal and External Reference.- 2.1.3 Multiplet Structure.- 2.1.4 Structure Dependence of the J-Coupling.- 2.1.5 Identification of Coupling Partners.- 2.1.6 Determination of Concentrations by NMR.- 2.1.7 Suppression of Strong Solvent Signals.- 2.2 Time-Dependent Processes in NMR.- 2.2.1 Correlation Time and Spectral Density.- 2.2.2 Chemical Exchange.- 2.2.3 pH-Dependence of the Chemical Shift.- 2.2.4 Formation of Complexes with Diamagnetic Ligands.- 2.2.5 Saturation Transfer.- 2.2.6 Nuclear Overhauser Effect.- 2.2.7 Labelling with Stable Isotopes.- 2.3 Two-Dimensional NMR Spectroscopy.- 2.3.1 The Two-Dimensional NMR Experiment.- 2.3.2 Interpretation of Homonuclear J-Coupling Patterns.- 2.3.3 Measurement of the Nuclear Overhauser Effect and Chemical Exchange.- 2.3.4 Correlation of Heteronuclear Resonances.- 3. NMR Spectroscopy of Biological Macromolecules.- 3.1 NMR Spectroscopy of Proteins.- 3.1.1 Composition and Structure of Proteins.- 3.1.2 Dynamical Processes in Proteins.- 3.1.3 Determination of Interatomic Distances.- 3.1.4 Assignment of Resonance Lines.- 3.1.5 Pattern Recognition in Two-Dimensional NMR Spectra.- 3.1.6 Structure Determination from NMR Data.- 3.1.7 Solid State NMR of Proteins.- 3.2 NMR Spectroscopy of Nucleic Acids, Polysaccharides and Lipids.- 3.2.1 Composition and Structure of Nucleic Acids.- 3.2.2 NMR Investigations of Nucleic Acids and Nucleic Acid Protein Complexes.- 3.2.3 Composition and Structure of Polysaccharides.- 3.2.4 Structure Determination of Polysaccharides.- 3.2.5 Investigations of Biological Membranes.- 4. NMR Tomography.- 4.1 Basic Principles of Imaging.- 4.1.1 Two-Dimensional Projection-Reconstruction.- 4.1.2 Two-Dimensional Fourier Imaging.- 4.1.3 Parameters of the NMR Tomogram.- 4.1.4 Methods for Reducing the Recording Time.- 4.1.5 Three-Dimensional Imaging.- 4.2 Some Applications of the Basic Experiments in NMR Tomography.- 4.2.1 Imaging of the Head.- 4.2.2 Imaging in Other Parts of the Body.- 4.3 Special Applications of NMR Tomography.- 4.3.1 Chemical Shift in Imaging.- 4.3.2 Flow Effects in NMR Tomography.- 4.3.3 Contrast Agents in NMR Tomography.- 4.3.4 NMR Microscopy.- 4.4 Biomedical Effects and Dangers of NMR.- 4.4.1 Biomedical Effects of the Static Magnetic Field.- 4.4.2 Biomedical Effects of Gradient Fields.- 4.4.3 Biomedical Effects of the Radio Frequency Field.- 5. Spatial Selective Spectroscopy and In Vivo NMR.- 5.1 Methods for Spatial Selection.- 5.1.1 Spatial Resolution with Isolated Cells and Organelles.- 5.1.2 Spatial Selection with Space Dependent Radio Frequency Fields.- 5.1.3 Spatial Selection with a Space Dependent Statistic Magnetic Field Bo.- 5.2 Typical Applications and Problems of NMR Spectroscopy in Living Systems.- 5.2.1 Preservation of the Natural Functions.- 5.2.2 In Vivo 1H-NMR Spectroscopy.- 5.2.3 In Vivo 31P-NMR Spectroscopy.- 5.2.4 In Vivo 13C-NMR Spectroscopy.- 5.2.5 In Vivo 15N-NMR Spectroscopy.- 5.2.6 In Vivo 19F-NMR Spectroscopy.- 5.2.7 In Vivo Spectroscopy with O