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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces

Gil Goobes1, Patrick S Stayton, Gary P Drobny

  • 1Department of Chemistry, University of Washington, Box 351700, Seattle WA 98195, USA, ggoobes@u.washington.edu , Tel: 1 (206) 543 7760.

Progress in Nuclear Magnetic Resonance Spectroscopy
|September 22, 2009
PubMed
Abstract

No abstract available in PubMed .

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Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
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