Rapid determination of protein global folds

Data processing: measuring – calibrating – or testing – Measurement system in a specific environment – Biological or biochemical

Reexamination Certificate

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C702S027000, 36, 36

Reexamination Certificate

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06882939

ABSTRACT:
This invention provides a method for rapidly obtaining accurate three-dimensional structure of proteins including large or multi-sub unit proteins, using a combination of NMR analysis of backbone only13C,15N or13C and15N isotopically labeled proteins which are optionally also2H isotopically labeled in the Cα position protons and residual dipolar coupling measurements in more than one partially aligned state and/or orientation data pertaining to overlapping successive peptide pairs.

REFERENCES:
patent: 5817474 (1998-10-01), Brown
patent: 6111066 (2000-08-01), Anderson, III et al.
patent: 6335196 (2002-01-01), Anderson, III et al.
patent: 6340578 (2002-01-01), Anderson, III et al.
Al-Hashimi et al J. Magnetic Resonance, 2000, vol. 143, 402-406.*
Mueller, G. et al Journal of Molecular Biology 2000, vol. 300(1), pp. 197-212.*
Ramirez et al., “Modulation of the Alignment Tensor of Macromolecules Dissolved in a Dilute Liquid Crystalline Medium,”J. Am. Chem. Soc.120:9106-9107, 1998.
Tjandra, et al., “Magnetic Field Dependence of Nitrogen-Proton J Splittings in15N-Enriched Human Ubiquitin Resulting from Relaxation . . . ,”J. Am. Chem. Soc., 118:6264-6272, 1996.
Bax et al., “High-Resolution Heteronuclear NMR of Human Ubiquitin in an Aqueous Liquid Crystalline Medium,”J. Biomol. NMR, 10:289-292, 1997.
Losonczi et al., “Improved Dilute Bicelle Solutions for High-Resolution NMR of Biological Macromolecules,”J. Biomol. NMR, 12:447-451 1998.
Prosser et al., “Use of a Novel Aqueous Liquid Crystalline Medium for High-Resolution NMR of Macromolecules in Solution,”J. Am. Chem. Soc.120:11010-11011, 1998.
Clore et al., “Measurement of Residual Dipolar Couplings of Macromolecules Aligned in the Nematic Phase of a Colloidal . . . ,”J. Am. Chem. Soc.120:10571-10572, 1998.
Hansen et al., “Tunable Alignment of Macromolecules by Filamentous Phage Yields Dipolar Coupling Interactions,”Nature Structural Biology5(12):1065-1074, 1998.
Kiddle et al., “Residual Dipolar Couplings as New Conformational Restraints in Isotopically13C-Enriched Oligosaccharides,”FEBS Letters436:128-130, 1998.
Wang et al., “A Liquid Crystalline Medium for Measuring Residual Dipolar Couplings Over a Wide Range of Temperatures,”J. Biomol. NMR, 12:443-446, 1998.
Ottiger et al., “Bicelle-Based Liquid Crystals for NMR-Measurement of Dipolar Couplings at Acidic and Basic pH Values,”J. Biomol. NMR, 13:187-191, 1999.
Fleming et al., “Cellulose Crystallites: A New and Robust Liquid Crystalline Medium for the Measurement of Residual Dipolar Couplings,”J. AM. Chem. Soc.122:5224-5225, 2000.
Rückert et al., “Alignment of Biological Macromolecules in Novel Nonionic Liquid Crystalline Media for NMR Experiments,”J. Am. Chem. Soc.122:7793-7797, 2000.
Mueller et al., “A Method for Incorporating Dipolar Couplings Into Structure Calculations in Cases of (Near) Axial Symmetry of Alignment,”J. Biomol. NMR18:183-188, 2000.
Hus et al., “De Novo Determination of Protein Structure by NMR Using Orientational and Long-Range Order Restraints,”J. Mol. Biol.298:927-936, 2000.
Tjandra et al., “Use of Dipolar1H-15N and1H-13C Couplings in the Structure Determination of Magnetically Oriented Macromolecules in Solution,”Nature Struct. Biol.4(9):732-738, 1997.
Wang et al., “Simultaneous Measurement1H-15N,1H-13C′and15N-13C′ Dipolar Couplings in a Perdeuterated 30 kDA Protein Dissolved in a Dilute Liquid Crystalline Phase,”J. Am. Chem. Soc.120:7385-7386, 1998.
Ottiger et al., “Measurement of J and Dipolar Couplings from Simplified Two-Dimensional NMR Spectra,”J. Magn. Reson.131:373-378, 1998.
Lerche et al., “Pulse Sequences for Measurement of One-Bond15N-1H Coupling Constants in the Protein Backbone,”J. Magn. Reson.140:259-263, 1999.
Tjandra et al., “Measurement of Dipolar Contributions to1JCH Splittings from Magnetic-Field Dependence of J Modulation in Two-Dimensional NMR Spectra,”J. Magn. Reson.124:512-515, 1997.
Clore et al., “Direct Structure Refinement Against Residual Dipolar Couplings in the Presence of Rhombicity of Unknown Magnitude,”J. Magn. Reson.131:159-162, 1998.
Clore et al., “A Robust Method for Determining the Magnitude of the Fully Asymmetric Alignment Tensor of Oriented Macromolecules in the Absence of Structural Information,”J. Magn. Reson.133:216-221, 1998.
Clore et al., “Impact of Residual Dipolar Couplings on the Accuracy of NMR Structures Determined from a Minimal Number of NOE Restraints,”J. Am. Chem. Soc.121:6513-6514, 1999.
Beger et al., “Protein φ and ψF0 Dihedral Restraints Determined from Multidimensional Hypersurface Correlations of Backbone Chemical Shifts and their Use in the Determination of Protein Tertiary Structures,”J. Biomol. NMR10:129-142, 1997.
Ottiger et al., “Determination of Relative N-HN, N-C′, Cα-C′, and Cα-Hαto Effective Bond Lengths in a Protein by NMR in a Dilute Liquid Crystalline Phase,”J. Am. Chem. Soc.120:12334-12341, 1998.
Ikura et al., “A Novel Approach for Sequential Assignment of1H,13C, and15N Spectra of Larger Proteins: Heteronuclear Triple-Resonance Three-Dimensional NMR Spectroscopy,”Biochemistry29:4659-4667, 1990.
Brünger, X-PLOR version 3.1: “A system for X-Ray Crystallography and NMR”, Yale University Press, New Haven, CT., v-xv,1987.
Losonczi et al., “Order Matrix Analysis of Residual Dipolar Couplings Using Singular Value Decomposition,”J. Magn. Reson.138:334-342, 1999.
Tolman et al., “Nuclear Magnetic Dipole Interactions in Field-Oriented Proteins: Information for Structure Determination in Solution”,Proc. Natl. Acad. Sci. USA92:9279-9283, 1995.
Tjandra et al., “Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium,”Science278:1111-1113, 1997.
Fowler et al., “Rapid Determination of Protein Folds Using Residual Dipolar Couplings,”J. Mol. Biol.304:447-460, 2000.
Hus et al., “Determination of Protein Backbone Structure Using Only Residual Dipolar Couplings,”J. Am. Chem. Soc.123:1541-1542, 2001.
Al-Hashimi et al., “Variation of Molecular Alignment as a Means of Resolving Orientational Ambiguities in Protein Structures from Dipolar Coupling,”J. Magn. Reson.143:402-406, 2000.
Mueller et al., “Global Folds of Proteins with Low Densities of NOEs Using Residual Dipolar Couplings: Application to the 370-Residue Maltodextrin-Binding Protein,”J. Mol. Biol.300:197-212, 2000.
McEvoy, Megan M., et al., “Nuclear Magnetic Resonance Assignments and Global Fold of a Chey-binding Domain in CheA, the Chemotaxis-Specific Kinase ofEscherichia Coli,” Biochemistry34(42):13871-13880, 1995. (Abstract).
Battiste, John L., et al., “Utilization of Site-Directed Spin Labeling and High-Resolution Nuclear Magnetic Resonance for Global Fold Determination of Large Proteins with Limited Nuclear Overhauser Effect Data,”Biochemistry39(18):5355-5365, May 9, 2000.

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