What can two-dimensional NMR tell us about proteins?
暂无分享,去创建一个
[1] K. Wüthrich,et al. Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy. , 1991, Journal of molecular biology.
[2] Klevit Re,et al. Two-dimensional 1H NMR studies of histidine-containing protein from Escherichia coli. 3. Secondary and tertiary structure as determined by NMR. , 1986 .
[3] Timothy F. Havel,et al. Three-dimensional solution structure of plastocyanin from the green alga Scenedesmus obliquus. , 1988, Science.
[4] 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.
[5] K Wüthrich,et al. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. , 1984, Journal of molecular biology.
[6] W. M. Westler,et al. Concerted two-dimensional NMR approaches to hydrogen-1, carbon-13, and nitrogen-15 resonance assignments in proteins. , 1989, Biochemistry.
[7] P E Wright,et al. Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. , 1988, Biochemistry.
[8] R. Lerner,et al. Isotope-edited NMR studies of Fab'-peptide complexes. , 1988, Peptide research.
[9] R. Huber,et al. Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A. , 1986, Journal of molecular biology.
[10] K Wüthrich,et al. Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the alpha-amylase inhibitor tendamistat. , 1986, Journal of molecular biology.
[11] C. Dobson,et al. Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. , 1988, Biochemistry.
[12] Ad Bax,et al. Three-dimensional heteronuclear NMR of nitrogen-15 labeled proteins , 1989 .
[13] M. Grady,et al. Tracing the sources , 1988, Nature.
[14] F. McCormick,et al. Identification of resonances from an oncogenic activating locus of human N-RAS-encoded p21 protein using isotope-edited NMR. , 1989, Proceedings of the National Academy of Sciences of the United States of America.
[15] S. Fesik,et al. Isotope-edited proton NMR study on the structure of a pepsin/inhibitor complex. , 1988, Biochemistry.
[16] M Karplus,et al. Application of molecular dynamics with interproton distance restraints to three-dimensional protein structure determination. A model study of crambin. , 1986, Journal of molecular biology.
[17] K. Wüthrich. Protein structure determination in solution by nuclear magnetic resonance spectroscopy. , 1989, Science.
[18] A. Gronenborn,et al. Solution structure of recombinant hirudin and the Lys-47----Glu mutant: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. , 1990, Biochemistry.
[19] C M Dobson,et al. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin. , 1989, Biochemistry.
[20] R. Kaptein,et al. Nonselective three-dimensional nmr spectroscopy. The 3D NOE-HOHAHA experiment , 1988 .
[21] K. Wüthrich,et al. Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance. , 1982, Journal of molecular biology.
[22] Timothy F. Havel,et al. Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. , 1987, Journal of molecular biology.
[23] W F van Gunsteren,et al. A protein structure from nuclear magnetic resonance data. lac repressor headpiece. , 1985, Journal of molecular biology.
[24] W. V. van Gunsteren,et al. Protein structures from NMR. , 1988, Biochemistry.
[25] A. Gronenborn,et al. Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. , 1988, Protein engineering.
[26] K Wüthrich,et al. Nuclear magnetic resonance identification of "half-turn" and 3(10)-helix secondary structure in rabbit liver metallothionein-2. , 1986, Journal of molecular biology.
[27] S. Fesik,et al. Heteronuclear three-dimensional NMR spectroscopy applied to CMP-KDO synthetase (27.5 kD). , 1989, Biochemical and biophysical research communications.
[28] Robert L. Baldwin,et al. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A , 1988, Nature.
[29] S. O. Smith,et al. High-resolution solid-state NMR of proteins. , 1988, Annual review of physical chemistry.
[30] G. Wagner,et al. Measurement of 13C relaxation times in proteins by two-dimensional heteronuclear 1H-13C correlation spectroscopy , 1988 .
[31] Y. Ovchinnikov,et al. Two‐dimensional 1H‐NMR study of bacterioopsin‐(34–65)‐polypeptide conformation , 1988 .
[32] P E Wright,et al. Three-dimensional solution structure of a single zinc finger DNA-binding domain. , 1989, Science.
[33] A. Schechter,et al. Reticulocyte Protein Synthesis: Response of Ribosome Fractions to Polyuridylic Acid , 1963, Science.
[34] A M Gronenborn,et al. Determination of three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy. , 1987, Protein engineering.
[35] K Wüthrich,et al. Determination of the complete three-dimensional structure of the alpha-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry. , 1988, Journal of molecular biology.
[36] I. Campbell,et al. 1H nuclear magnetic resonance studies of an integral membrane protein: subunit c of the F1F0 ATP synthase. , 1987, Journal of molecular biology.
[37] Timothy F. Havel,et al. A distance geometry program for determining the structures of small proteins and other macromolecules from nuclear magnetic resonance measurements of intramolecular1H−1H proximities in solution , 1984 .
[38] J. Guss,et al. Structure of oxidized poplar plastocyanin at 1.6 A resolution. , 1983, Journal of molecular biology.
[39] P. Wright,et al. Complete assignment of the 1H nuclear magnetic resonance spectrum of French bean plastocyanin. Sequential resonance assignments, secondary structure and global fold. , 1988, Journal of molecular biology.
[40] P. Wright,et al. 1H NMR studies of human C3a anaphylatoxin in solution: sequential resonance assignments, secondary structure, and global fold. , 1988, Biochemistry.
[41] S. Walter Englander,et al. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR , 1988, Nature.
[42] L. Delbaere,et al. Tertiary structure of histidine-containing protein of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli. , 1987, The Journal of biological chemistry.
[43] W. Braun,et al. Distance geometry and related methods for protein structure determination from NMR data , 1987, Quarterly Reviews of Biophysics.
[44] N Go,et al. Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm. , 1985, Journal of molecular biology.
[45] P. Kraulis,et al. Three-dimensional NMR spectroscopy of a protein in solution , 1988, Nature.
[46] A M Gronenborn,et al. Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. , 1989, Biochemistry.