NMR analysis of a 900K GroEL–GroES complex
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Kurt Wüthrich | Jocelyne Fiaux | K. Wüthrich | J. Fiaux | A. Horwich | E. Bertelsen | Arthur L. Horwich | Eric B. Bertelsen | Jocelyne Fiaux
[1] K. Wüthrich. NMR of proteins and nucleic acids , 1988 .
[2] Zbyszek Otwinowski,et al. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å , 1994, Nature.
[3] K Wüthrich,et al. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[4] J. Deisenhofer,et al. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution , 1996, Nature.
[5] K. Wüthrich,et al. Digital filtering with a sinusoidal window function: An alternative technique for resolution enhancement in FT NMR , 1976 .
[6] Geoffrey I. Webb,et al. NMR of proteins and nucleic acids , 2005 .
[7] F. Dahlquist,et al. Large modular proteins by NMR , 1997, Nature Structural Biology.
[8] R. Riek,et al. Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[9] R. Glockshuber,et al. Pilus chaperone FimC–adhesin FimH interactions mapped by TROSY-NMR , 1999, Nature Structural Biology.
[10] K Wüthrich,et al. NMR spectroscopy of large molecules and multimolecular assemblies in solution. , 1999, Current opinion in structural biology.
[11] K Wüthrich,et al. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules , 1995, Journal of biomolecular NMR.
[12] J. Weissman,et al. Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. , 1998, Methods in Enzymology.
[13] J. Weissman,et al. Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes , 1995, Cell.
[14] A. Horwich,et al. Structure and function in GroEL-mediated protein folding. , 1998, Annual review of biochemistry.
[15] D. J. Naylor,et al. Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding , 2001, Cell.
[16] Helen R Saibil,et al. The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL , 1996, Cell.
[17] J. Weissman,et al. Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction , 1996, Cell.
[18] G. Roberts,et al. Mobility of polypeptide chain in the pyruvate dehydrogenase complex revealed by proton NMR , 1981, Nature.
[19] Gareth A. Morris,et al. Enhancement of nuclear magnetic resonance signals by polarization transfer , 1979 .
[20] Lila M. Gierasch,et al. Characterization of a functionally important mobile domain of GroES , 1993, Nature.
[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] M. Goldman,et al. Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei , 1984 .
[23] F. Shewmaker,et al. The Disordered Mobile Loop of GroES Folds into a Defined β-Hairpin upon Binding GroEL* , 2001, The Journal of Biological Chemistry.
[25] Kurt Wüthrich,et al. Processing of multi-dimensional NMR data with the new software PROSA , 1992 .
[26] F. Hartl,et al. Protein folding in the central cavity of the GroEL–GroES chaperonin complex , 1996, Nature.
[27] R. Riek,et al. TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. , 2000, Trends in biochemical sciences.
[28] Kurt Wüthrich,et al. TROSY-TYPE TRIPLE-RESONANCE EXPERIMENTS FOR SEQUENTIAL NMR ASSIGNMENTS OF LARGE PROTEINS , 1999 .
[29] A. Horwich,et al. The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex , 1997, Nature.
[30] C. Georgopoulos,et al. Interplay of structure and disorder in cochaperonin mobile loops. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[31] I. Shimada,et al. Nuclear magnetic resonance study of antibodies: a multinuclear approach. , 1994, Methods in enzymology.