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Nuclear magnetic resonance identification of "half-turn" and 3(10)-helix secondary structure in rabbit liver metallothionein-2 (Q70033259)

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scientific article published on 01 January 1986

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English	Nuclear magnetic resonance identification of "half-turn" and 3(10)-helix secondary structure in rabbit liver metallothionein-2	scientific article published on 01 January 1986

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8 October 2019

Nuclear magnetic resonance identification of "half-turn" and 3(10)-helix secondary structure in rabbit liver metallothionein-2 (English)

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8 October 2019

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K Wüthrich

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8 October 2019

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G Wagner

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8 October 2019

D Neuhaus

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8 October 2019

E Wörgötter

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8 October 2019

M Vasák

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8 October 2019

J H Kägi

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publication date

1 January 1986

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8 October 2019

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5

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Journal of Molecular Biology

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8 October 2019

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8 October 2019

1

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8 October 2019

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8 October 2019

Structure of apamin in solution: a two-dimensional nuclear magnetic resonance study

1 reference

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Beta-hairpin families in globular proteins

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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

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A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

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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

1 reference

9 October 2022

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Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution

1 reference

9 October 2022

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Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances

1 reference

9 October 2022

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Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins

1 reference

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Calibration of the angular dependence of the amide proton-C alpha proton coupling constants, 3JHN alpha, in a globular protein. Use of 3JHN alpha for identification of helical secondary structure

1 reference

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The anatomy and taxonomy of protein structure

1 reference

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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 elucidat

1 reference

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Secondary structure in the solution conformation of the proteinase inhibitor IIA from bull seminal plasma by nuclear magnetic resonance.

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Secondary structure of the alpha-amylase polypeptide inhibitor tendamistat from Streptomyces tendae determined in solution by 1H nuclear magnetic resonance

1 reference

9 October 2022

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Identifiers

10.1016/0022-2836(86)90413-4

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8 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

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8 October 2019

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