Projects per year
Abstract
alpha-Helical coiled coils are ubiquitous protein-protein-interaction domains. They share a relatively straightforward sequence repeat, which directs the folding and assembly of amphipathic helices. The helices can combine in a number of oligonnerisation states and topologies to direct a wide variety of protein assemblies. Although in nature parallel dimers, trimers and tetramers dominate, the potential to form larger oligomers and more-complex assemblies has long been recognised. In particular, complexes above pentamer are interesting because they are barrel-like, having central channels or pores with well-defined dimensions and chemistry. Recent empirical and rational design experiments are beginning to chart this potential new territory in coiled-coil space, leading to intriguing new structures, and possibilities for functionalisation and applications.
Original language | English |
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Pages (from-to) | 432-441 |
Number of pages | 10 |
Journal | Current Opinion in Structural Biology |
Volume | 22 |
Issue number | 4 |
DOIs | |
Publication status | Published - Aug 2012 |
Research Groups and Themes
- Bristol BioDesign Institute
Keywords
- synthetic biology
- MECHANOSENSITIVE CHANNEL
- ANGSTROM RESOLUTION
- CRYSTAL-STRUCTURE
- SYNTHETIC BIOLOGY
- MEMBRANE-PROTEIN
- GCN4 LEUCINE-ZIPPER
- PACKING
- DESIGN
- PROTEIN STRUCTURES
- BURIED POLAR RESIDUES
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Dive into the research topics of 'New currency for old rope: from coiled-coil assemblies to alpha-helical barrels'. Together they form a unique fingerprint.Projects
- 2 Finished
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Electron Delocalization in Peptides and Proteins
Woolfson, D. N. (Principal Investigator)
1/10/11 → 1/10/14
Project: Research
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A BIOMOLECULAR-DESIGN APPROACH IN SYNTHETIC BIOLOGY: TOWARDS SYNTHETIC CYTOSKELETONS
Woolfson, D. N. (Principal Investigator)
1/07/09 → 1/07/13
Project: Research