NMR for Chemists and Biologists by Rodrigo J CarbajoNMR for Chemists and Biologists by Rodrigo J Carbajo

NMR for Chemists and Biologists

byRodrigo J Carbajo, Jose L Neira

Paperback | July 4, 2013

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This book intends to be an easy and concise introduction to the field of nuclear magnetic resonance or NMR, which has revolutionized life sciences in the last twenty years. A significant part of the progress observed in scientific areas like Chemistry, Biology or Medicine can be ascribed to the development experienced by NMR in recent times. Many of the books currently available on NMR deal with the theoretical basis and some of its main applications, but they generally demand a strong background in Physics and Mathematics for a full understanding. This book is aimed to a wide scientific audience, trying to introduce NMR by making all possible effort to remove, without losing any formality and rigor, most of the theoretical jargon that is present in other NMR books. Furthermore, illustrations are provided that show all the basic concepts using a naive vector formalism, or using a simplified approach to the particular NMR-technique described. The intention has been to show simply the foundations and main concepts of NMR, rather than seeking thorough mathematical expressions.
Title:NMR for Chemists and BiologistsFormat:PaperbackDimensions:115 pagesPublished:July 4, 2013Publisher:Springer-Verlag/Sci-Tech/TradeLanguage:English

The following ISBNs are associated with this title:

ISBN - 10:940076975X

ISBN - 13:9789400769755

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Table of Contents

1. The basis of Nuclear Magnetic Resonance Spectroscopy1.1. Introduction1.2. Physical principles of NMR spectroscopy1.2.1. The basis of NMR spectroscopy: a vector approach1.2.2. The basis of NMR spectroscopy: a naïve quantum approach1.2.3. The nuclei in NMR1.3. Spin relaxation1.3.1. Spin-lattice relaxation time1.3.2. Spin-spin relaxation time1.3.3. Sources of variation in local fields1.4. Pulse techniques1.4.1. How a pulse works: the time and frequency domains1.4.2. Multipulse experiments: measurement of the T1- and T2-relaxation times as examples1.5. Practical aspects of NMR1.5.1. The magnet1.5.2. The probe1.5.3. The lock-system1.5.4. The transmitter/receiver system: quadrature detection1.5.5. The shim system1.5.6. Pulse field gradients1.5.7. Sample preparation1.6. References 2. Spectroscopic parameters in Nuclear Magnetic Resonance2.1. The chemical shift and the spectral intensity2.1.1. The shielding screening constant2.1.2. The chemical shift2.1.3. Signal intensity2.2. The scalar coupling constant2.2.1. Spin-spin coupling2.2.2. How does spin-spin coupling occur?2.2.3. Variations in the value of J2.2.4. Spin-spin decoupling2.3. The nuclear Overhauser effect2.3.1. The basis of the NOE: a two spin system2.3.2. NOEs in multi-spin systems2.4. References  3. Basic NMR experiments3.1. Introduction3.2. 1D NMR 3.2.1. Sensitivity and frequency3.2.2. Acquisition and processing3.2.3. 1D spectra of 1H, 13C,31P and 19F3.3. Multidimensional NMR3.3.1. Generating dimensions in NMR3.3.2. 2D data acquisition and processing 3.4. Homonuclear shift correlation: correlations through the chemical bond3.4.1. COSY. Experiment interpretation and practical aspects3.4.2. TOCSY. Practical aspects 3.4.3. Correlation for diluted spins: the INADEQUATE experiment. Double-quantum selection3.5. Heteronuclear shift correlation: correlations through the chemical bond3.5.1. Polarization transfer experiments: SPT and INEPT sequences; indirect spectroscopy3.5.2. Heteronuclear single bond correlations: HSQC and HMQC3.5.3. Double resonance experiments: homonuclear spin decoupling; heteronuclear double resonance and broadband decoupling3.6. Correlations through space3.6.1. Steady-state NOE3.6.2. Kinetic or transient NOE3.6.3. The 2D-NOESY sequence and practical aspects of the experiment3.7. References 4. Biomolecular NMR4.1. Introduction4.2. Why biomolecules? Main applications4.3. Structure of biomolecules4.3.1. Homonuclear and heteronuclear (triple resonance) assignment in proteins4.3.2. Nucleic acids4.4. Biomolecular dynamics4.4.1. Comparison with other spectroscopies and other structural biophysical techniques4.4.2. Movements in the ps-s range 4.5. Biomolecular interactions (NMR in drug discovery)4.5.1. Order of the affinities measured4.5.2. Experiments in NMR screening 4.6. Other applications4.6.1. Metabolomics4.6.2. Solid state NMR and HR-MAS4.7. References