Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.

[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.