Physics of NMR Spectroscopy in Biology and MedicineB. Maraviglia Elsevier, 1 sept. 1988 - 483 pages As a result of the recent expansion of nuclear magnetic resonance in biomedicine, a number of workshops and schools have been organized to introduce the NMR principles to a wider group of biologists, radiologists, neurologists, etc. The aim of most of these courses was to provide a common vocabulary and enough information about ``pulse sequences'', relaxation times, etc. in order to facilitate the use of the various types of NMR imaging systems. However, no courses were organized for the physicists who were responsible for the origin and evolution of the ideas in this area. This Enrico Fermi school was therefore organized. The topics discussed included the theoretical interpretation and prediction of NMR signals, the study of new imaging techniques up to the building of special r.f. coils and the study of new methods for analysing NMR data in the time domain. |
Table des matières
| 1 | |
Chapter 2 Lectures on pulsed NMR | 43 |
Chapter 3 NMR studies of membranes and whole cells | 121 |
Chapter 4 A brief account of twodimensional NMR spectroscopy | 158 |
Chapter 5 Magnetic relaxation of smallmolecule nuclear spins in colloid systems | 186 |
Chapter 6 Magicangle sample spinning | 203 |
Chapter 7 Determination of the solution structure of proteins from NMR | 267 |
Chapter 8 NMR studies of cholesterol orientational order and dynamics and the phase equilibria of cholesterolphospholipid mixtures | 302 |
Chapter 10 Principles of NMR imaging | 345 |
T1 and T2 dependence | 370 |
Chapter 12 Macromolecular spatial distribution by NMR | 382 |
Chapter 13 In vivo NMR spectroscopy | 389 |
Chapter 14 Sensitivity probe design and spatial localization for in vivo NMR | 412 |
Chapter 15 Standardization in medical and biological NMR studies | 440 |
Chapter 16 The contrasttonoise and signaltonoise ratios in MRI | 451 |
Chapter 9 Quantitative analysis of NMR signals in the time domain | 313 |
Autres éditions - Tout afficher
Expressions et termes fréquents
2H NMR amplitude average axis calculated centerband Chem chemical shift chemical-shift cholesterol coherence transfer component constraints correlation corresponding decay decoupling defined density matrix depends deuterium difierent dipolar couplings distance domain double-quantum echo efiect energy equation evolution excitation experiment experimental first fit fitting flip angle Fourier transform frequency gradient Hamiltonian heteronuclear high-field HSVD intensity interactions isotropic Larmor frequency linear LPSVD Magn magnetic field MASS spectrum membranes method model function molecular molecules motion multiple-quantum NMR imaging NMR spectra nuclei obtained one-quantum operator orientation parameters peaks phase phospholipid Phys precession probe profile protein proton pulse sequence quadrupolar quantum r.f. field region relaxation resonance rotating frame rotor sample selection shown in fig sidebands signal significant sinusoids slice solid spatial specific spectra spectroscopy spectrum spin system spin temperature spin-lattice relaxation structure surface coil symmetry tensor tissue transitions two-dimensional vector voxel Zeeman zero zero-field