Spatial structure of rabbit liver metallothionein-2 in solution by NMR.

[1]  K. Wüthrich,et al.  Sequence-specific 1H-NMR assignments in rabbit-liver metallothionein-2. , 1986, European journal of biochemistry.

[2]  K Wüthrich,et al.  Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution. , 1986, Journal of molecular biology.

[3]  R. R. Ernst,et al.  Polypeptide-metal cluster connectivities in metallothionein 2 by novel proton-cadmium-113 heteronuclear two-dimensional NMR experiments , 1985 .

[4]  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.

[5]  Timothy F. Havel,et al.  Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry. , 1985, Journal of molecular biology.

[6]  P. Sadler,et al.  113Cd NMR studies of reconstituted seven-cadmium metallothionein: evidence for structural flexibility. , 1985, Biochemistry.

[7]  K. Wüthrich,et al.  113CD-1H spin-spin couplings in homonuclear 1H correlated spectroscopy of metallothionein. Identification of the cysteine 1H spin systems. , 1984, European journal of biochemistry.

[8]  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.

[9]  K Wüthrich,et al.  Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor. , 1982, Journal of molecular biology.

[10]  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.

[11]  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.

[12]  A. Dubs,et al.  Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor. , 1979, Biochimica et biophysica acta.

[13]  R. R. Ernst,et al.  Two‐dimensional spectroscopy. Application to nuclear magnetic resonance , 1976 .

[14]  J. L. Bethune,et al.  Equine hepatic and renal metallothioneins. Purification, molecular weight, amino acid composition, and metal content. , 1974, The Journal of biological chemistry.

[15]  L. Berliner,et al.  Biological Magnetic Resonance , 1987, Springer US.

[16]  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 .

[17]  J. Otvos,et al.  Principles and Applications of 113Cd NMR to Biological Systems , 1982 .

[18]  N. Otaki,et al.  Rabbit liver metallothionein. Tentative amino acid sequence of metallothionein-B. , 1979, Experientia. Supplementum.