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The design of antiparallel coiled coils
Current Opinion in Structural Biology, 2001Recent structural studies have highlighted the importance of antiparallel coiled coils in nature. In addition, well-behaved, model antiparallel coiled coils have been designed and used for the reassembly of protein fragments and for the study of the energetic contributions of various interactions to helix orientation specificity.
M G, Oakley, J J, Hollenbeck
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A Coiled Coil with a Fluorous Core
Journal of the American Chemical Society, 2001The design, synthesis, and structural characterization of a highly fluorinated peptide system based on the coiled coil region of the yeast transcription factor GCN4 is described. All four leucine residues (a position) and three valine residues (d position) were replaced by the unnatural amino acids 5,5,5-trifluoroleucine and 4,4,4-trifluorovaline ...
B, Bilgiçer, A, Fichera, K, Kumar
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The Structure of α-Helical Coiled Coils
2005alpha-Helical coiled coils are versatile protein domains, supporting a wide range of biological functions. Their fold is probably better understood than that of any other protein; indeed, uniquely among folds, their structure can be computed from a set of parametric equations. Here, we review the principles of coiled-coil structure, the determinants of
Lupas, A. ; https://orcid.org/0000-0002-1959-4836 +1 more
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Coiled coils meet the chaperone world
Trends in Biochemical Sciences, 2004Coiled coils are versatile structural modules that engage in a variety of cellular activities. Recent studies illuminate their role as substrate-binding elements in the chaperone cofactor prefoldin and in the AAA+ ATPases involved in protein (un)folding processes.
Martin, J. ; https://orcid.org/0000-0003-1398-0274 +2 more
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Short Homodimeric and Heterodimeric Coiled Coils
Biomacromolecules, 2006In this communication, we discuss the design, synthesis, and characterization of four peptides which are able to self-assemble into five different homo- and heterodimeric alpha-helical coiled coils based on the pH of their environment. These peptides are very short, containing only 14 or 21 amino acids each, and illustrate the minimum requirements ...
He, Dong, Jeffrey D, Hartgerink
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Predicting coiled-coil regions in proteins
Current Opinion in Structural Biology, 1997The past several years have seen significant advances in our ability to recognize coiled coils from protein sequences and model their structures. New methods include a detection program based on pairwise residue correlations, a program that distinguishes two-stranded from three-stranded coiled coils and a routine for modelling the coordinates of the ...
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Engineered Coiled-Coil Protein Microfibers
Biomacromolecules, 2014The fabrication of de novo proteins able to self-assemble on the nano- to meso-length scales is critical in the development of protein-based biomaterials in nanotechnology and medicine. Here we report the design and characterization of a protein engineered coiled-coil that not only assembles into microfibers, but also can bind hydrophobic small ...
Jasmin, Hume +7 more
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Coiled-coils and fibrous proteins
Journal of Structural Biology, 2010David A D, Parry, John M, Squire
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Coiled-Coil Design: Updated and Upgraded
2017α-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 ...
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