Angular Restraints from Residual Dipolar Couplings for Structure Refinement

Griesinger, Christian; Meiler, Jens; Peti, Wolfgang

doi:10.1007/0-306-47936-2_7

Christian Griesinger³,
Jens Meiler^3,4 &
Wolfgang Peti^3,5

Part of the book series: Biological Magnetic Resonance ((BIMR,volume 20))

198 Accesses
6 Citations

Abstract

Dipolar couplings have proven to provide long range restraints before not available in high resolution NMR. This review presents an overview of recent techniques for the measurement of dipolar couplings. A special focus on side chain and proton-proton dipolar couplings can be found. The second part centers on the use of dipolar couplings in structure calculations of proteins and carbohydrates. Their usage in a 3D homology search and structural genomic efforts using NMR are also discussed.

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Group 030, Max Planck Institute of Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany
Christian Griesinger, Jens Meiler & Wolfgang Peti
Department of Biochemistry, University of Washington, Box 357350, Seattle, Wa, 98195, USA
Jens Meiler
Department of Molecular Biology, The Scripps Research Institute, MB-44, 10550 North Torrey Pines Road, La Jolla, Ca, 92037, USA
Wolfgang Peti

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University of Alabama at Birmingham, Birmingham, Alabama
N. Rama Krishna
University of Denver, Denver, Colorado
Lawrence J. Berliner

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Griesinger, C., Meiler, J., Peti, W. (2002). Angular Restraints from Residual Dipolar Couplings for Structure Refinement. In: Krishna, N.R., Berliner, L.J. (eds) Protein NMR for the Millennium. Biological Magnetic Resonance, vol 20. Springer, Boston, MA. https://doi.org/10.1007/0-306-47936-2_7

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