Rapid Protein Structure Detection and Assignment using Residual Dipolar Couplings
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[1] Rolf Boelens,et al. Graph-theoretical assignment of secondary structure in multidimensional protein NMR spectra: Application to the lac repressor headpiece , 1995, Journal of biomolecular NMR.
[2] P. Kraulis,et al. Protein three-dimensional structure determination and sequence-specific assignment of 13C and 15N-separated NOE data. A novel real-space ab initio approach. , 1994, Journal of molecular biology.
[3] K. Wüthrich. NMR of proteins and nucleic acids , 1988 .
[4] L. Mueller,et al. Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions , 1998, Nature Structural Biology.
[5] Ad Bax,et al. Four-Dimensional 15N-Separated NOESY of Slowly Tumbling Perdeuterated 15N-Enriched Proteins. Application to HIV-1 Nef , 1995 .
[6] J. Struppe,et al. Dilute bicellar solutions for structural NMR work. , 1998, Journal of magnetic resonance.
[7] Rafael Brüschweiler,et al. Assignment strategy for proteins with known structure. , 2002, Journal of magnetic resonance.
[8] G T Montelione,et al. Automated analysis of nuclear magnetic resonance assignments for proteins. , 1995, Current opinion in structural biology.
[9] Werner Braun,et al. Automated combined assignment of NOESY spectra and three-dimensional protein structure determination , 1997, Journal of biomolecular NMR.
[10] A. Bax,et al. Delineation of .alpha.-helical domains in deuteriated Staphylococcal nuclease by 2D NOE NMR spectroscopy , 1988 .
[11] P. Güntert. Structure calculation of biological macromolecules from NMR data , 1998, Quarterly Reviews of Biophysics.
[12] Chris Bailey-Kellogg,et al. The NOESY Jigsaw: Automated Protein Secondary Structure and Main-Chain Assignment from Sparse, Unassigned NMR Data , 2000, J. Comput. Biol..
[13] G. Montelione,et al. Automated analysis of protein NMR assignments using methods from artificial intelligence. , 1997, Journal of molecular biology.
[14] Structural constraints from residual tensorial couplings in high resolution NMR without an explicit term for the alignment tensor , 1999, Journal of biomolecular NMR.
[15] Eva Thulin,et al. Recognition of protein folds via dipolar couplings , 1999 .
[16] Mark J Howard,et al. Protein NMR spectroscopy , 1998, Current Biology.
[17] Harold A. Scheraga,et al. Exact solutions for chemical bond orientations from residual dipolar couplings , 2002, Journal of biomolecular NMR.
[18] W. Braun,et al. Automated assignment of simulated and experimental NOESY spectra of proteins by feedback filtering and self-correcting distance geometry. , 1995, Journal of molecular biology.
[19] D. Baker,et al. De novo determination of protein backbone structure from residual dipolar couplings using Rosetta. , 2002, Journal of the American Chemical Society.
[20] L. Kay,et al. Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR. , 1997, Biochemistry.
[21] A. Bax,et al. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. , 1997, Science.
[22] J. Hus,et al. Determination of protein backbone structure using only residual dipolar couplings. , 2001, Journal of the American Chemical Society.
[23] Gordon M. Crippen,et al. Distance Geometry and Molecular Conformation , 1988 .
[24] J H Prestegard,et al. Variation of molecular alignment as a means of resolving orientational ambiguities in protein structures from dipolar couplings. , 2000, Journal of magnetic resonance.
[25] J H Prestegard,et al. Order matrix analysis of residual dipolar couplings using singular value decomposition. , 1999, Journal of magnetic resonance.
[26] D. M. Schneider,et al. Implementation of the main chain directed assignment strategy. Computer assisted approach. , 1991, Biophysical journal.
[27] A M Gronenborn,et al. A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. , 1998, Journal of magnetic resonance.
[28] Horst Kessler,et al. Automated backbone assignment of labeled proteins using the threshold accepting algorithm , 1998, Journal of biomolecular NMR.
[29] P. Hajduk,et al. Discovering High-Affinity Ligands for Proteins , 1997, Science.
[30] H Oschkinat,et al. Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin. , 1997, Journal of molecular biology.