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Science 24 December 1993:
Vol. 262. no. 5142, pp. 2005 - 2009
DOI: 10.1126/science.8266096
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Articles

Science, Vol 262, Issue 5142, 2005-2009
Copyright © 1993 by American Association for the Advancement of Science

articles

Generation of impossible cross-peaks between bulk water and biomolecules in solution NMR

WS Warren, W Richter, AH Andreotti, and BT Farmer 2nd

Department of Chemistry, Princeton University, NJ 08544-1009.

Intermolecular multiple-quantum coherences between bulk water and a glycoprotein fragment at modest concentration (20 mM) have been experimentally produced and detected, although such coherences are inconceivable in the normal theoretical framework of nuclear magnetic resonance. A density matrix treatment explains these results by including the long-range dipolar interaction between spins and by discarding the high-temperature approximation. These results imply that peak intensities (critical for structural determinations) can be distorted in many gradient experiments, and show that magic-angle gradients provide substantial improvements with reduced gradient strengths. They also suggest methods for contrast enhancement in magnetic resonance imaging.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Accurate Temperature Imaging Based on Intermolecular Coherences in Magnetic Resonance.
G. Galiana, R. T. Branca, E. R. Jenista, and W. S. Warren (2008)
Science 322, 421-424
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Confinement Effect on Dipole-Dipole Interactions in Nanofluids.
J. Baugh, A. Kleinhammes, D. Han, Q. Wang, and Y. Wu (2001)
Science 294, 1505-1507
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Resurrection of Crushed Magnetization and Chaotic Dynamics in Solution NMR Spectroscopy.
Y.-Y. Lin, N. Lisitza, S. Ahn, and W. S. Warren (2000)
Science 290, 118-121
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Structure of the Membrane Domain of Subunit b of the Escherichia coli F0F1 ATP Synthase.
O. Dmitriev, P. C. Jones, W. Jiang, and R. H. Fillingame (1999)
J. Biol. Chem. 274, 15598-15604
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Imaging with intermolecular multiple-quantum coherences in solution nuclear magnetic resonance.
W Richter, S Lee, W. Warren, and Q He (1995)
Science 267, 654-657
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Structure of Ala20right-arrow Pro/Pro64right-arrow Ala Substituted Subunit c of Escherichia coli ATP Synthase in Which the Essential Proline Is Switched between Transmembrane Helices.
O. Y. Dmitriev and R. H. Fillingame (2001)
J. Biol. Chem. 276, 27449-27454
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