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Subcell Biochem. 2017;82:35-61. doi: 10.1007/978-3-319-49674-0_2.

Coiled-Coil Design: Updated and Upgraded.

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School of Chemistry, University of Bristol, BS8 1TS, Bristol, UK.
School of Biochemistry, University of Bristol, BS8 1TD, Bristol, UK.
BrisSynBio, Life Sciences Building, University of Bristol, BS8 1TQ, Bristol, UK.


α-Helical coiled coils are ubiquitous protein-folding and protein-interaction domains in which two or more α-helical chains come together to form bundles. Through a combination of bioinformatics analysis of many thousands of natural coiled-coil sequences and structures, plus empirical protein engineering and design studies, there is now a deep understanding of the sequence-to-structure relationships for this class of protein architecture. This has led to considerable success in rational design and what might be termed in biro de novo design of simple coiled coils, which include homo- and hetero-meric parallel dimers, trimers and tetramers. In turn, these provide a toolkit for directing the assembly of both natural proteins and more complex designs in protein engineering, materials science and synthetic biology. Moving on, the increased and improved use of computational design is allowing access to coiled-coil structures that are rare or even not observed in nature, for example α-helical barrels, which comprise five or more α-helices and have central channels into which different functions may be ported. This chapter reviews all of these advances, outlining improvements in our knowledge of the fundamentals of coiled-coil folding and assembly, and highlighting new coiled coil-based materials and applications that this new understanding is opening up. Despite considerable progress, however, challenges remain in coiled-coil design, and the next decade promises to be as productive and exciting as the last.


Coiled coil; Computational design; De novo design; Peptide assembly; Protein design; Protein engineering

[Indexed for MEDLINE]

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