Magnetic resonance force microscopy
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Magnetic resonance force microscopy (MRFM) is an imaging technique that acquires magnetic resonance images (MRI) at nanometer scales, and possibly at atomic scales in the future. MRFM is potentially able to observe protein structures which cannot be seen using X-ray crystallography and protein nuclear magnetic resonance spectroscopy. Detection of the magnetic spin of a single electron has been demonstrated using this technique. The sensitivity of a current MRFM microscope is 10 billion times better than a medical MRI used in hospitals.
Magnetic Resonance Force Microscopy (MRFM) is a measurement technique conceived to observe the three-dimensional atomic structures of single molecules. The concept combines the ideas of magnetic resonance imaging (MRI) and atomic force microscopy (AFM). Conventional MRI employs an inductive coil as an antenna to sense resonant nuclear or electronic spins in a magnetic field gradient. MRFM uses magnet-tipped cantilever to directly detect a modulated spin gradient force between sample spins and the tip. Unlike the inductive coil approach, MRFM sensitivity scales favorably as device dimensions are made smaller.
The basic principles of MRFM imaging and the theoretical possibility of this technology were first described in 1991. The first MRFM image was obtained in 1993 at the IBM Almaden Research Center with 1-μm vertical resolution and 5-μm lateral resolution using a bulk sample of the paramagnetic substance . The spatial resolution reached nanometer-scale in 2003. Detection of the magnetic spin of a single electron was achieved in 2004.
- University of Washington Quantum System Engineering and MRFM Home Page, http://courses.washington.edu/goodall/MRFM/.
- Magnetic-Resonance Force Microscopy, http://www.medgadget.com/archives/2005/04/magneticresonan.html.
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Categories: Microscopes | Nuclear magnetic resonance | Protein structure | Nanotechnology