Nuclear magnetic resonance at very high field strengths can give a wealth of information about macromolecules, though there are still limitations to the size of globular protein which it can handle.
HIGH-resolution nuclear magnetic resonance spectroscopy affords a uniquely penetrating method of studying co-ordinate complex formation between boron trifluoride and electron donor substances.
The Nuclear Magnetic Resonance Core supports MSK researchers by providing essential analytical services, access and education for analytical instrumentation and related shared scientific resources.
Nuclear Magnetic Resonance (NMR) was first experimentally observed in late 1945, nearly simultaneously by the research groups of Felix Bloch, at Stanford University and Edward Purcell at Harvard ...
Equipped with 600 MHz and 700MHz spectrometers equipped with a salt-tolerant 13C-enhanced triple resonance cryo-probe, a 1H,13C capillary flow probe and liquid handling robot and a 1.7mm ...
Nuclear magnetic resonance (NMR) is ubiquitous in chemistry and materials science. One of the reasons for its widespread popularity is because NMR is able to provide valuable information on the ...
The CU Boulder Biochemistry Nuclear Magnetic Resonance (NMR) facility located in JSCBB serves the research needs of the entire campus community as well as outside research entities, both public and ...
This NMR Facility has capabilities for solution-state, solid-state, gaseous-state, rheo, diffusion, and MRI (magnetic resonance imaging). A short introduction to NMR spectroscopy can be found here.
The Nuclear Magnetic Resonance Spectroscopy Lab features a state-of-the-art JEOL 400 MHz NMR equipped with auto sampling and automatic tuning & matching. The instrument can perform temperature and ...