The DOI matches its Crossref record; 158 of the 158 references it cites were found in a registry or an index.
Coiled-Coil Design: Updated and Upgraded
Abstract
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.
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“Since there is a small spacing deviation between 3.5 in heptad repeats and 3.6 in ideal α-helices, the hydrophobic face of a helix with 3.5 spacing proceeds around the helix, leading to supercoiling of helices upon assembly rather than packing in a straight manner.6”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [6]
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Metadata
- Authors
- Woolfson, D. N.
- Affiliations
- University of Bristol (GB)
- Corresponding author
- Woolfson, Derek N.
- ORCID
- Woolfson, Derek N.
- Venue
- Subcellular Biochemistry
- Publisher
- Springer International Publishing
- Published
- 2017
- Volume
- 82
- Pages
- 35-61
- ISSN
- 0306-0225 (ISSN-L)
- OpenAlex
- W2579233876
- Cited by
- 149
- References
- 158
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 14 · 2023: 24 · 2022: 18 · 2021: 27 · 2020: 18 · 2019: 9 · 2018: 16 · 2017: 9
- FWCI
- 17.68
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Sub-cellular biochemistry/Subcellular biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Explore Bristol Research (submittedVersion)
- Bristol Research (University of Bristol) (submittedVersion)
- Funders
- Biotechnology and Biological Sciences Research Council (BB/L01386X/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Keywords
- alpha-helical coiled coil, protein folding, protein-protein interaction domains, rational protein design, de novo protein design, protein assembly, synthetic biology, protein-based materials
- MeSH terms
- Protein Conformation, alpha-Helical, Animals, Humans, Models, Molecular, Proteins, Protein Folding, Protein Interaction Domains and Motifs
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