Solution structure and backbone dynamics of an ω‐conotoxin precursor
暂无分享,去创建一个
Gerhard Wagner | G. Wagner | D. Goldenberg | David P. Goldenberg | Rachel E. Koehn | Dara E. Gilbert | D. Gilbert | Rachel E. Koehn
[1] J. Rivier,et al. Conotoxin MI. Disulfide bonding and conformational states. , 1983, The Journal of biological chemistry.
[2] Timothy F. Havel,et al. NMR structure determination in solution: a critique and comparison with X-ray crystallography. , 1992, Annual review of biophysics and biomolecular structure.
[3] K. Wüthrich. NMR of proteins and nucleic acids , 1988 .
[4] M. Adams,et al. CALCIUM CHANNEL DIVERSITY AND NEUROTRANSMITTER RELEASE : THE OMEGA -CONOTOXINS AND OMEGA -AGATOXINS , 1994 .
[5] K. Wüthrich,et al. Use of amide 1H‐nmr titration shifts for studies of polypeptide conformation , 1979 .
[6] A. Gronenborn,et al. Analysis of the backbone dynamics of interleukin-1.beta. using two-dimensional inverse detected heteronuclear nitrogen-15-proton NMR spectroscopy , 1990 .
[7] V. Saudek,et al. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions , 1992, Journal of biomolecular NMR.
[8] V. Basus,et al. Solution structure of ω‐conotoxin MVIIA using 2D NMR spectroscopy , 1995 .
[9] A. Szabó,et al. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results , 1982 .
[10] Ad Bax,et al. Quantitative J correlation: a new approach for measuring homonuclear three-bond J(HNH.alpha.) coupling constants in 15N-enriched proteins , 1993 .
[11] A. Gronenborn,et al. Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy. , 1990, Biochemistry.
[12] T. Oas,et al. Determinants of backbone dynamics in native BPTI: cooperative influence of the 14-38 disulfide and the Tyr35 side-chain. , 1998, Journal of molecular biology.
[13] Giovanni Lipari,et al. MODEL-FREE APPROACH TO THE INTERPRETATION OF NUCLEAR MAGNETIC RESONANCE RELAXATION IN MACROMOLECULES. 1. THEORY AND RANGE OF VALIDITY , 1982 .
[14] T. Pawson,et al. Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. , 1994, Biochemistry.
[15] H. Scheraga,et al. Disulfide bonds and protein folding. , 2000, Biochemistry.
[16] F. Studier,et al. Use of T7 RNA polymerase to direct expression of cloned genes. , 1990, Methods in enzymology.
[17] C. Pace,et al. Hydrogen bonding stabilizes globular proteins. , 1996, Biophysical journal.
[18] D. Craik,et al. A consensus structure for omega-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: comparison of MVIIA, SVIB and SNX-202. , 1996, Journal of molecular biology.
[19] R. Norton,et al. Roles of key functional groups in omega-conotoxin GVIA synthesis, structure and functional assay of selected peptide analogues. , 1999, European journal of biochemistry.
[20] Folding of omega-conotoxins. 1. Efficient disulfide-coupled folding of mature sequences in vitro. , 1996, Biochemistry.
[21] J. Lefèvre,et al. Structural and dynamic characterization of omega-conotoxin MVIIA: the binding loop exhibits slow conformational exchange. , 2000, Biochemistry.
[22] Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease. , 1995, Biochemistry.
[23] A. Arseniev,et al. Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy. , 1994, European journal of biochemistry.
[24] D. Goldenberg,et al. Folding of omega-conotoxins. 2. Influence of precursor sequences and protein disulfide isomerase. , 1996, Biochemistry.
[25] J. McIntosh,et al. Neuronal calcium channel antagonists. Discrimination between calcium channel subtypes using omega-conotoxin from Conus magus venom. , 1987, Biochemistry.
[26] J. Gavilanes,et al. Characterization of pKa values and titration shifts in the cytotoxic ribonuclease alpha-sarcin by NMR. Relationship between electrostatic interactions, structure, and catalytic function. , 1998, Biochemistry.
[27] T Szyperski,et al. Protein dynamics studied by rotating frame 15N spin relaxation times , 1993, Journal of biomolecular NMR.
[28] K. Wüthrich,et al. Torsion angle dynamics for NMR structure calculation with the new program DYANA. , 1997, Journal of molecular biology.
[29] D. Craik,et al. Effects of chirality at Tyr13 on the structure-activity relationships of omega-conotoxins from Conus magus. , 1999, Biochemistry.
[30] B. Olivera,et al. A novel D-leucine-containing Conus peptide: diverse conformational dynamics in the contryphan family. , 1999, The journal of peptide research : official journal of the American Peptide Society.
[31] A. Palmer,et al. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. , 1995, Journal of molecular biology.
[32] A. Palmer,et al. Dynamics of ribonuclease H: temperature dependence of motions on multiple time scales. , 1996, Biochemistry.
[33] S. Woodward,et al. Constant and hypervariable regions in conotoxin propeptides. , 1990, The EMBO journal.
[34] J. Ramachandran,et al. Antagonists of neuronal calcium channels: structure, function, and therapeutic implications. , 1995, Annual review of pharmacology and toxicology.
[35] B. Eipper,et al. Identification of subcellular compartments containing peptidylglycine alpha-amidating monooxygenase in rat anterior pituitary. , 1995, Journal of cell science.
[36] T. Kohno,et al. Three-dimensional structure in solution of the calcium channel blocker omega-conotoxin MVIIA. , 1995, Biochemistry.
[37] Yawen Bai,et al. Primary structure effects on peptide group hydrogen exchange , 1993, Biochemistry.
[38] J. Imperial,et al. Precursor structure of ω-conotoxin GVIA determined from a cDNA clone , 1992 .
[39] M. Takahashi,et al. Tyr13 is essential for the activity of omega-conotoxin MVIIA and GVIA, specific N-type calcium channel blockers. , 1995, Biochemical and biophysical research communications.
[40] L. Kay,et al. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. , 1989, Biochemistry.
[41] D. Goldenberg,et al. Roles of individual disulfide bonds in the stability and folding of an omega-conotoxin. , 1998, Biochemistry.
[42] R. Mains,et al. Peptidylglycine α‐amidating monooxygenase: A multifunctional protein with catalytic, processing, and routing domains , 1993, Protein science : a publication of the Protein Society.
[43] S. Grzesiek,et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.
[44] J. Lefèvre,et al. Theory and practice of nuclear spin relaxation in proteins. , 1996, Annual review of physical chemistry.
[45] K. Tarczy-Hornoch,et al. Structure-activity analysis of a Conus peptide blocker of N-type neuronal calcium channels. , 1995, Biochemistry.
[46] R. Luther,et al. Pharmacotherapeutic potential of omega-conotoxin MVIIA (SNX-111), an N-type neuronal calcium channel blocker found in the venom of Conus magus. , 1998, Toxicon : official journal of the International Society on Toxinology.
[47] P. S. Kim,et al. Formation of a native‐like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor , 1994, Protein science : a publication of the Protein Society.
[48] Toshiomi Yoshida,et al. Solution Structure of ω-Conotoxin MVIIC Determinined by NMR , 1995 .
[49] K Wüthrich,et al. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules , 1995, Journal of biomolecular NMR.
[50] A. Szabó,et al. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity , 1982 .
[51] J. H. Strange,et al. Studies of chemical exchange by nuclear magnetic relaxation in the rotating frame , 1970 .
[52] D. Merkler,et al. C-terminal amidated peptides: production by the in vitro enzymatic amidation of glycine-extended peptides and the importance of the amide to bioactivity. , 1994, Enzyme and microbial technology.
[53] S. Woodward,et al. Diversity of Conus neuropeptides. , 1990, Science.
[54] M. Billeter,et al. MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.
[55] G. Wagner,et al. Relaxation-Rate Measurements for 15N−1H Groups with Pulsed-Field Gradients and Preservation of Coherence Pathways , 1994 .
[56] V L Arcus,et al. pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds. , 1995, Biochemistry.
[57] K. Yutani,et al. Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. , 1999, Biochemistry.
[58] A. Bax,et al. An alternative 3D NMR technique for correlating backbone 15N with side chain Hβ resonances in larger proteins , 1991 .
[59] J Ramachandran,et al. Solution structure of omega-conotoxin GVIA using 2-D NMR spectroscopy and relaxation matrix analysis. , 1993, Biochemistry.