Nuclear magnetic resonance (NMR) is an effect whereby magnetic nuclei in a magnetic field absorb and re-emit electromagnetic (EM) energy. This energy is at a specific resonance frequency which depends on the strength of the magnetic field and other factors. This allows the observation of specific quantum mechanical magnetic properties of an atomic nucleus.
Many scientific techniques exploit NMR phenomena to study molecular physics, crystals and non-crystalline materials through NMR spectroscopy. NMR is also routinely used in advanced medical imaging techniques, such as in magnetic resonance imaging (MRI).
How does it work?The versatility of NMR spectroscopy has made it a widespread tool in chemistry for the study of chemical structure. In additional to the one-dimensional NMR spectroscopy used to study chemical bonds, two dimensional approaches have been developed for the determination of the structure of complex molecules like proteins. Time domain NMR spectroscopy is used to study molecular dynamics in solutions. NMR of solid samples can help determine molecular structures. There are NMR methods for measuring diffusion coefficients.
NMR spectroscopy has contributed enormously to chemical knowledge. A wide range of techniques has been used with a range of magnetic fields including high-field superconducting magnets. NMR frequencies from 60 to 800 MHz have been used for hydrogens, compared to the range of about 15 to 300 MHz for medical magnetic resonance imaging (MRI). One of the major sources of chemical information is the measurement of chemical shifts in high-resolution NMR spectroscopy. The chemical shifts are a very sensitive probe of the chemical environment of the resonating nuclei.
Chemical analysis of liquids and dissolved solids; kinetic and temperature studies of reaction mixtures; characterisation of polymers including structure, co-monomer ratios, end groups; average molecular weight; molecular dynamics; protein folding; ionization; protein hydration; hydrogen bonding; drug screening and design; native membrane protein; metabolite analysis.
Sample Handling Requirements:
Deuterated solvent solution.
Various spectrometers, up to a maximum field frequency of 700 MHz, Bruker Avance 700
Dr Ian Hancox, 024 76 150380 email i dot hancox at warwick dot ac dot uk.
Typical results format, and sample:
|Warwick collect/analyse data|
|Warwick collect data|
|Available to user with expertise/ contribution|
||Spare capacity for collaborative research|