Protein NMR spectroscopy in structural genomics

Protein NMR spectroscopy provides an important complement to X-ray crystallography for structural genomics, both for determining three-dimensional protein structures and in characterizing their biochemical and biophysical functions.

[1]  M. Billeter,et al.  Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals , 1992, Quarterly Reviews of Biophysics.

[2]  C Sander,et al.  Mapping the Protein Universe , 1996, Science.

[3]  J. Reuben,et al.  Biological Magnetic Resonance , 1983, Springer US.

[4]  Arthur G. Palmer,et al.  Nuclear Magnetic Resonance Studies of Biopolymer Dynamics , 1996 .

[5]  S. Grzesiek,et al.  Direct Observation of Hydrogen Bonds in Proteins by Interresidue 3hJNC' Scalar Couplings , 1999 .

[6]  H N Moseley,et al.  Automated analysis of NMR assignments and structures for proteins. , 1999, Current opinion in structural biology.

[7]  Kurt Wüthrich,et al.  The second decade — into the third millenium , 1998, Nature Structural Biology.

[8]  A G Murzin,et al.  SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.

[9]  P. Hajduk,et al.  Discovering High-Affinity Ligands for Proteins: SAR by NMR , 1996, Science.

[10]  J. Skolnick,et al.  Method for prediction of protein function from sequence using the sequence-to-structure-to-function paradigm with application to glutaredoxins/thioredoxins and T1 ribonucleases. , 1998, Journal of molecular biology.

[11]  A. Bax,et al.  Protein backbone angle restraints from searching a database for chemical shift and sequence homology , 1999, Journal of biomolecular NMR.

[12]  W. Hendrickson Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. , 1991, Science.

[13]  David C. Jones,et al.  CATH--a hierarchic classification of protein domain structures. , 1997, Structure.

[14]  K Wüthrich,et al.  NMR spectroscopy of large molecules and multimolecular assemblies in solution. , 1999, Current opinion in structural biology.

[15]  J. Prestegard,et al.  New techniques in structural NMR — anisotropic interactions , 1998, Nature Structural Biology.

[16]  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.

[17]  L. Berliner,et al.  Biological Magnetic Resonance , 1987, Springer US.

[18]  A. Bax,et al.  Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. , 1997, Science.

[19]  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.

[20]  Thomas Szyperski,et al.  Sequential resonance assignment of medium-sized15 N/13C-labeled proteins with projected 4D triple resonance NMR experiments , 1998 .

[21]  R. Riek,et al.  Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[22]  Jeanmarie Guenot,et al.  Variability of conformations at crystal contacts in BPTI represent true low‐energy structures: Correspondence among lattice packing and molecular dynamics structures , 1992, Proteins.

[23]  L. Mueller,et al.  Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions , 1998, Nature Structural Biology.

[24]  G. Wider,et al.  Reduced dimensionality in triple-resonance NMR experiments , 1993 .