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

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8 October 2019

title

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

6

K Wüthrich

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8 October 2019

author name string

G Wagner

1

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8 October 2019

D Neuhaus

2

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8 October 2019

E Wörgötter

3

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8 October 2019

M Vasák

4

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8 October 2019

J H Kägi

5

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8 October 2019

publication date

1 January 1986

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Journal of Molecular Biology

8 October 2019

number of pages

5

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based on heuristic

inferred from page(s)

published in

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8 October 2019

volume

187

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8 October 2019

issue

1

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8 October 2019

page(s)

131-135

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

8 October 2019

cites work

1 reference

9 October 2022

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Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance

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Beta-hairpin families in globular proteins

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9 October 2022

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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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9 October 2022

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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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9 October 2022

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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

https://opencitations.net/index/coci/api/v1/references/10.1016/0022-2836(86)90413-4

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

1 reference

9 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0022-2836(86)90413-4

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

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9 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0022-2836(86)90413-4

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

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9 October 2022

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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

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9 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0022-2836(86)90413-4

The anatomy and taxonomy of protein structure

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9 October 2022

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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

9 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0022-2836(86)90413-4

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

1 reference

9 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0022-2836(86)90413-4

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

https://opencitations.net/index/coci/api/v1/references/10.1016/0022-2836(86)90413-4

Identifiers

DOI

10.1016/0022-2836(86)90413-4

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8 October 2019

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