Secondary structure of acyl carrier protein as derived from two-dimensional 1H NMR spectroscopy.
暂无分享,去创建一个
[1] K Wüthrich,et al. Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance. , 1982, Journal of molecular biology.
[2] G. Bodenhausen,et al. Exploring nuclear spin systems by relayed magnetization transfer , 1982 .
[3] Kurt Wüthrich,et al. Homonuclear two-dimensional 1H NMR of proteins. Experimental procedures , 1984 .
[4] D. States,et al. A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants☆ , 1982 .
[5] Ad Bax,et al. Investigation of complex networks of spin-spin coupling by two-dimensional NMR , 1981 .
[6] Kurt Wüthrich,et al. Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 2. Combined use of correlated spectroscopy and nuclear Overhauser spectroscopy for sequential assignments of backbone resonances and elucidation of polypeptide secondary structures. , 1981, European journal of biochemistry.
[7] Richard R. Ernst,et al. Investigation of exchange processes by two‐dimensional NMR spectroscopy , 1979 .
[8] K. Wüthrich,et al. Improved spectral resolution in cosy 1H NMR spectra of proteins via double quantum filtering. , 1983, Biochemical and biophysical research communications.
[9] G. Wider,et al. Assignment of the 1H nuclear magnetic resonance spectrum of the proteinase inhibitor IIA from bull seminal plasma by two-dimensional nuclear magnetic resonance at 500 MHz. , 1983, Journal of molecular biology.
[10] C. Dobson,et al. Assignment of resonances in the 1H NMR spectrum of human lysozyme. , 1985, European journal of biochemistry.
[11] D. Wemmer,et al. Proton NMR studies of .lambda. cro repressor. 2. Sequential resonance assignments of the proton NMR spectrum , 1985 .
[12] J. Richardson,et al. Preliminary X-ray diffraction studies of acyl carrier protein from Escherichia coli. , 1985, Journal of molecular biology.
[13] Kurt Wüthrich,et al. Secondary structure of the α-amylase polypeptide inhibitor Tendamistat from Streptomyces tendae determined in solution by 1H nuclear magnetic resonance , 1985 .
[14] Kurt Wüthrich,et al. Experimental techniques of two-dimensional correlated spectroscopy , 1980 .
[15] H. Schulz. On the structure-function relationship of acyl carrier protein of Escherichia coli. , 1975, The Journal of biological chemistry.
[16] K Wüthrich,et al. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. , 1984, Journal of molecular biology.
[17] 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.
[18] J. Elovson,et al. Acyl carrier protein. XI. The specificity of acyl carrier protein synthetase. , 1969, Journal of Biological Chemistry.
[19] K Wüthrich,et al. Systematic application of high-resolution, phase-sensitive two-dimensional 1H-NMR techniques for the identification of the amino-acid-proton spin systems in proteins. Rabbit metallothionein-2. , 1985, European journal of biochemistry.
[20] K Wüthrich,et al. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. , 1980, Biochemical and biophysical research communications.
[21] R. R. Ernst,et al. Two‐dimensional spectroscopy. Application to nuclear magnetic resonance , 1976 .
[22] C. Tanford,et al. Gross conformation of Escherichia coli acyl carrier protein. , 1968, The Journal of biological chemistry.
[23] K Wüthrich,et al. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor. , 1982, Journal of molecular biology.
[24] K. Wüthrich,et al. Secondary structure of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[25] S. Wakil,et al. The preparation of tryptic, peptic, thermolysin, and cyanogen bromide peptides from the acyl carrier protein of Escherichia coli. , 1968, The Journal of biological chemistry.
[26] Prescott Dj,et al. Acyl Carrier Protein , 1972 .
[27] S. Wakil,et al. The complete amino acid sequence of the acyl carrier protein of Escherichia coli. , 1968, Journal of Biological Chemistry.
[28] K Wüthrich,et al. Sequential individual resonance assignments in the 1H‐NMR spectra of polypeptides and proteins , 1983, Biopolymers.
[29] J. Prestegard,et al. Acyl carrier protein from Escherichia coli I. Aspects of the solution structure as evidenced by proton nuclear Overhauser experiments at 500 MHz. , 1983, Biochemistry.
[30] S. Wakil,et al. Fatty acid synthesis and its regulation. , 1983, Annual review of biochemistry.
[31] 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.
[32] A. Bax,et al. Optimization of two-dimensional homonuclear relayed coherence transfer NMR spectroscopy , 1985 .
[33] A. Wand,et al. Two-dimensional 1H NMR studies of cytochrome c. , 1985, Biochemistry.
[34] C. Rock,et al. Re-evaluation of the solution structure of acyl carrier protein. , 1979, The Journal of biological chemistry.
[35] K. Wüthrich,et al. Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy. , 1983, European journal of biochemistry.
[36] P. Y. Chou,et al. Empirical predictions of protein conformation. , 1978, Annual review of biochemistry.
[37] C. Rock,et al. Improved purification of acyl carrier protein. , 1980, Analytical biochemistry.
[38] K Wüthrich,et al. Secondary structure in the solution conformation of the proteinase inhibitor IIA from bull seminal plasma by nuclear magnetic resonance. , 1984, Journal of molecular biology.