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Nuclear magnetic resonance identification of “half-turn” and 310-helix secondary structure in rabbit liver metallothionein-2

Data up to Jan 2025

Published1986
Citations197
References16

Total Citations Per Year

Abstract

References (16)

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

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

1986 • 142 citations

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1983 • 100 citations

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

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Nuclear magnetic resonance identification of “half-turn” and 310-helix secondary… (1986) – Journal of Molecular Biology | Metascience Observatory Explorer