Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.
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[1] H N Moseley,et al. Automated analysis of NMR assignments and structures for proteins. , 1999, Current opinion in structural biology.
[2] Patrice Koehl,et al. Linear Prediction Spectral Analysis of NMR Data , 1999 .
[3] Kurt Wüthrich,et al. TROSY-TYPE TRIPLE-RESONANCE EXPERIMENTS FOR SEQUENTIAL NMR ASSIGNMENTS OF LARGE PROTEINS , 1999 .
[4] G. Montelione,et al. The structure of the N-terminus of striated muscle alpha-tropomyosin in a chimeric peptide: nuclear magnetic resonance structure and circular dichroism studies. , 1998, Biochemistry.
[5] Thomas Szyperski,et al. Sequential resonance assignment of medium-sized15 N/13C-labeled proteins with projected 4D triple resonance NMR experiments , 1998 .
[6] L. Kay,et al. The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. , 1998, Annual review of biophysics and biomolecular structure.
[7] G. Montelione,et al. A novel RNA-binding motif in influenza A virus non-structural protein 1 , 1997, Nature Structural Biology.
[8] G T Montelione,et al. High-resolution solution NMR structure of the Z domain of staphylococcal protein A. , 1997, Journal of molecular biology.
[9] R. Powers,et al. Assignments, secondary structure and dynamics of the inhibitor-free catalytic fragment of human fibroblast collagenase , 1997, Journal of biomolecular NMR.
[10] G. Montelione,et al. Automated analysis of protein NMR assignments using methods from artificial intelligence. , 1997, Journal of molecular biology.
[11] G. Montelione,et al. Phase labeling of C−H and C−C spin-system topologies: Application in constant-time PFG-CBCA(CO)NH experiments for discriminating amino acid spin-system types , 1996, Journal of biomolecular NMR.
[12] G. Montelione,et al. Phase labeling of C−H and C−C spin-system topologies: Application in PFG-HACANH and PFG-HACA(CO)NH triple-resonance experiments for determining backbone resonance assignments in proteins , 1996, Journal of biomolecular NMR.
[13] G. Montelione,et al. Classification of amino acid spin systems using PFG HCC(CO)NH-TOCSY with constant-time aliphatic 13C frequency labeling , 1995, Journal of biomolecular NMR.
[14] Eric Oldfield,et al. 1H, 13C and 15N chemical shift referencing in biomolecular NMR , 1995, Journal of biomolecular NMR.
[15] L. Kay,et al. Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution. , 1995, Progress in biophysics and molecular biology.
[16] D. Wishart,et al. The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data , 1994, Journal of biomolecular NMR.
[17] G T Montelione,et al. An improved strategy for determining resonance assignments for isotopically enriched proteins and its application to an engineered domain of staphylococcal protein A. , 1993, Biochemistry.
[18] L. Kay. Pulsed-field gradient-enhanced three-dimensional NMR experiment for correlating 13C.alpha./.beta., 13C', and 1H.alpha. chemical shifts in uniformly carbon-13-labeled proteins dissolved in water , 1993 .
[19] Ad Bax,et al. Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins , 1993, Journal of biomolecular NMR.
[20] Gaetano T. Montelione,et al. An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins , 1992 .
[21] W. M. Westler,et al. A relational database for sequence-specific protein NMR data , 1991, Journal of biomolecular NMR.
[22] A M Gronenborn,et al. Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. , 1991, Science.
[23] L. Kay,et al. A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. , 1990, Biochemistry.
[24] L. Kay,et al. A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin , 1990 .
[25] Paul C. Driscoll,et al. Practical aspects of proton-carbon-carbon-proton three-dimensional correlation spectroscopy of 13C-labeled proteins , 1990 .
[26] G. Montelione,et al. Conformation-independent sequential NMR connections in isotope-enriched polypeptides by 1H13C15N triple-resonance experiments , 1990 .
[27] K. Wüthrich. NMR of proteins and nucleic acids , 1988 .
[28] K Wüthrich,et al. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor. , 1982, Journal of molecular biology.
[29] K Wüthrich,et al. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations. , 1982, Journal of molecular biology.