ChemInform Abstract: Nuclear Magnetic Resonance: A Tool for Structural Biology

The 'Beginner's Guides' are an ongoing series of feature articles, each one covering a key technique and offering the scientifically literate, but not necessarily expert audience, a background briefing on the underlying science of a technique that is (or will be) widely used in molecular bioscience. The series will cover a mixture of techniques, including some that are well established amongst a subset of our readership but not necessarily familiar to those in different specialisms. This 'Beginner's Guide' covers nuclear magnetic resonance. Nuclear magnetic resonance (NMR) provides a way to explore the 3D structures of macromolecules in much more biologically relevant conditions and does this by taking advantage of the quantum mechanical property of some nuclei---nuclear spin. Here, we discuss how nuclear spin can be harnessed to provide information on the 3D structure of macromolecules in solution and how new thinking is leading to a revolution in drug discovery.

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Magic-Angle Spinning Solid-State Nuclear Magnetic Resonance: Application to Structural Biology

Encyclopedia of Analytical Chemistry ◽

10.1002/9780470027318.a9036 ◽

2009 ◽

Cited By ~ 1

Author(s):

Amir Goldbourt

Keyword(s):

Nuclear Magnetic Resonance ◽

Solid State ◽

Magnetic Resonance ◽

Structural Biology ◽

Magic Angle Spinning ◽

Magic Angle ◽

Angle Spinning ◽

Nuclear Magnetic

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Nuclear magnetic resonance analysis of protein–DNA interactions

Journal of The Royal Society Interface ◽

10.1098/rsif.2010.0543 ◽

2011 ◽

Vol 8 (61) ◽

pp. 1065-1078 ◽

Cited By ~ 21

Author(s):

S. Campagne ◽

V. Gervais ◽

A. Milon

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Structural Biology ◽

Molecular Mechanisms ◽

Nuclear Magnetic Resonance Analysis ◽

Macromolecular Complexes ◽

Resonance Analysis ◽

Protein Dna Interactions ◽

Experimental Strategies ◽

Nuclear Magnetic

Recent methodological and instrumental advances in solution-state nuclear magnetic resonance have opened up the way to investigating challenging problems in structural biology such as large macromolecular complexes. This review focuses on the experimental strategies currently employed to solve structures of protein–DNA complexes and to analyse their dynamics. It highlights how these approaches can help in understanding detailed molecular mechanisms of target recognition.

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An emerging technology: Nuclear magnetic resonance microscopy

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010010706x ◽

1988 ◽

Vol 46 ◽

pp. 1000-1001

Author(s):

M.J. Hennessy ◽

E. Kwok

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Relaxation Times ◽

Basic Research ◽

Local Environment ◽

Magnetic Resonance Images ◽

Nmr Microscopy ◽

Mri Scans ◽

Temperature Relaxation ◽

Nuclear Magnetic

Much progress in nuclear magnetic resonance microscope has been made in the last few years as a result of improved instrumentation and techniques being made available through basic research in magnetic resonance imaging (MRI) technologies for medicine. Nuclear magnetic resonance (NMR) was first observed in the hydrogen nucleus in water by Bloch, Purcell and Pound over 40 years ago. Today, in medicine, virtually all commercial MRI scans are made of water bound in tissue. This is also true for NMR microscopy, which has focussed mainly on biological applications. The reason water is the favored molecule for NMR is because water is,the most abundant molecule in biology. It is also the most NMR sensitive having the largest nuclear magnetic moment and having reasonable room temperature relaxation times (from 10 ms to 3 sec). The contrast seen in magnetic resonance images is due mostly to distribution of water relaxation times in sample which are extremely sensitive to the local environment.

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Nuclear magnetic resonance microscopy

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100156110 ◽

1989 ◽

Vol 47 ◽

pp. 828-829

Author(s):

Paul C. Lauterbur

Keyword(s):

Magnetic Field ◽

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Magnetic Fields ◽

Signal To Noise ◽

Field Gradients ◽

Useful Signal ◽

Magnetic Field Gradients ◽

Observation Times ◽

Nuclear Magnetic

Nuclear magnetic resonance imaging can reach microscopic resolution, as was noted many years ago, but the first serious attempt to explore the limits of the possibilities was made by Hedges. Resolution is ultimately limited under most circumstances by the signal-to-noise ratio, which is greater for small radio receiver coils, high magnetic fields and long observation times. The strongest signals in biological applications are obtained from water protons; for the usual magnetic fields used in NMR experiments (2-14 tesla), receiver coils of one to several millimeters in diameter, and observation times of a number of minutes, the volume resolution will be limited to a few hundred or thousand cubic micrometers. The proportions of voxels may be freely chosen within wide limits by varying the details of the imaging procedure. For isotropic resolution, therefore, objects of the order of (10μm) may be distinguished.Because the spatial coordinates are encoded by magnetic field gradients, the NMR resonance frequency differences, which determine the potential spatial resolution, may be made very large. As noted above, however, the corresponding volumes may become too small to give useful signal-to-noise ratios. In the presence of magnetic field gradients there will also be a loss of signal strength and resolution because molecular diffusion causes the coherence of the NMR signal to decay more rapidly than it otherwise would. This phenomenon is especially important in microscopic imaging.

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