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Understanding membrane protein structure by design

Nature Structural Biology volume 7, pages 91–94 (2000)Cite this article

Abstract

In contrast to soluble proteins, the primary interactions that specify and stabilize membrane protein structures are still largely a matter of speculation. Although van der Waals interactions have been gaining increasing favor as the dominant player, new results demonstrate the strength of hydrogen bonding in a membrane environment.

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Figure 1: The GCN4 leucine zipper.
Figure 2: Comparison of the glycophorin A transmembrane helix dimer and the GCN4-LZ dimer structures.

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Authors and Affiliations

  1. the Department of Chemistry and Biochemistry and Laboratory of Structural Biology and Molecular Medicine, MBI, University of California, 611 Charles E. Young Dr. E., Los Angeles, Los Angeles, 90095-1570, California, USA

    James U. Bowie

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  1. James U. Bowie
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Bowie, J. Understanding membrane protein structure by design. Nat Struct Mol Biol 7, 91–94 (2000). https://doi.org/10.1038/72454

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