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- W2020861880 abstract "Analysis of 1H-1H nuclear Overhauser effects and amide proton-C alpha proton coupling constants in rabbit liver metallothionein-2 resulted in the identification of two segments of 3(10)-helix and numerous secondary structure elements of a novel type, which we call half-turn. A half-turn can be generated starting from a type II tight turn by rotation of phi 3 from +90 degrees to -90 degrees. Its appearance in metallothionein appears to be a consequence of the constraints on the polypeptide conformation by the large number of metal binding sites." @default.
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- W2020861880 date "1986-01-01" @default.
- W2020861880 modified "2023-10-10" @default.
- W2020861880 title "Nuclear magnetic resonance identification of “half-turn” and 310-helix secondary structure in rabbit liver metallothionein-2" @default.
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- W2020861880 doi "https://doi.org/10.1016/0022-2836(86)90413-4" @default.
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