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Ionic Crystal Structures

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Related Experiment Video

Updated: Jul 22, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

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Structural relationships in the two-zinc insulin hexamer.

E J Dodson, G G Dodson, D C Hodgkin

Canadian Journal of Biochemistry

|June 1, 1979

Summary

Detailed analysis of two-Zn pig insulin reveals structural similarities and differences between its two independent molecules. Conformational flexibility may influence insulin's biological activity.

Area of Science:

Biochemistry
Structural Biology
Crystallography

Background:

Insulin's structure is crucial for its biological function.
Understanding insulin's conformational states is key to its activity.

Purpose of the Study:

To refine the crystal structure of two-Zn pig insulin.
To compare the two independent molecules within the insulin dimer.
To describe molecular interactions at monomer, dimer, and hexamer levels.

Main Methods:

X-ray crystallography with 1.5-Å resolution data.
Fourier and fast Fourier least-squares refinement methods.

Main Results:

High agreement in main chain structures between the two molecules, with exceptions at A-chain N-terminus and B-chain C-terminus.

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Close adherence to two-fold symmetry along local axes, except for B25 side chain.

Greater structural discrepancies observed away from the symmetry axis.

Conclusions:

The two independent molecules in the two-Zn insulin dimer exhibit high structural similarity.
Insulin's capacity for conformational variation is likely significant for its biological activity.