Determination of residual dipolar couplings in homonuclear MOCCA-SIAM experiments |
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Authors: | Möglich Andreas Wenzler Michael Kramer Frank Glaser Steffen J Brunner Eike |
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Institution: | (1) Institute of Biophysics and Physical Biochemistry, University of Regensburg, D-93040 Regensburg, Germany;(2) Institute of Organic Chemistry and Biochemistry II, Technical University of Munich, D-85747 Garching, Germany |
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Abstract: | In solutions with partial molecular alignment, anisotropic magnetic interactions such as the chemical shift anisotropy, the electric quadrupole interaction, and the magnetic dipole-dipole interaction are no longer averaged out to zero in contrast to isotropic solutions. The resulting residual anisotropic magnetic interactions are increasingly used in biological NMR studies for the determination of 3D structures of proteins and other biomolecules. In the present paper we propose a new approach allowing the measurement of residual HN-H dipolar couplings of non-isotope enriched proteins based on the application of the MOCCA-SIAM experiment. This experiment allows the measurement of homonuclear coupling constants with an accuracy of ca. ±0.2 Hz and is therefore particularly well suited to determine residual dipolar couplings at relatively low degrees of molecular orientation. The agreement between experimentally determined residual HN-H couplings and calculated values is demonstrated for BPTI. |
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Keywords: | MOCCA mixing sequence NMR protein structure residual dipolar couplings SIAM experiment |
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