Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation |
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Authors: | Kloiber Karin Schüler Wolfgang Konrat Robert |
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Institution: | (1) Protein Engineering Network Centers of Excellence and Department of Medical Genetics and Microbiology, Biochemistry and Chemistry, University of Toronto, Toronto, Ontario, Canada, M5S 1A8;(2) ProCeryon Biosciences GmbH, Jakob Haringer Strasse 3, A-5020 Salzburg, Austria;(3) Institute of Theoretical Chemistry and Molecular Structural Biology, University of Vienna, Rennweg 95b, Austria |
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Abstract: | The simultaneous interpretation of a suite of dipole-dipole and dipole-CSA cross-correlation rates involving the backbone nuclei 13C, 1H,13CO, 15N and 1HN can be used to resolve the ambiguities associated with each individual cross-correlation rate. The method is based on the transformation of experimental cross-correlation rates via calculated values based on standard peptide plane geometry and solid-state 13CO CSA parameters into a dihedral angle probability surface. Triple resonance NMR experiments with improved sensitivity have been devised for the quantification of relaxation interference between 1H(i)-13C(i)/15N(i)-1HN(i) and 1H(i–1)-13C(i–1)/15N(i)-1HN(i) dipole-dipole mechanisms in 15N,13C-labeled proteins. The approach is illustrated with an application to 13C,15N-labeled ubiquitin. |
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Keywords: | chemical shift anisotropy cross-correlated spin relaxation dihedral angles multiple-quantum coherence NMR spectroscopy protein structure determination |
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