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• W2019935314 abstract "The coiled coil is one of the most common protein-structure motifs. It is believed to be adopted by 3–5% of all amino acids in proteins. It comprises two or more α-helical chains wrapped around one another. The sequences of most coiled coils are characterized by a seven-residue (heptad) repeat, denoted (abcdefg)n. Residues at the a and d positions define the helical interface (core) and are usually hydrophobic, though about 20% are polar or charged. We show that parallel coiled-coils have a unique pattern of their negatively charged residues at the core positions: aspartic acid is excluded from these positions while glutamic acid is not. In contrast the antiparallel structures are more permissive in their amino acid usage. We show further, and for the first time, that incorporation of Asp but not Glu into the a positions of a parallel coiled coil creates a flexible hinge and that the maximal hinge angle is being directly related to the number of incorporated mutations. These new computational and experimental observations will be of use in improving protein-structure predictions, and as rules to guide rational design of novel coiled-coil motifs and coiled coil-based materials." @default.
• W2019935314 created "2016-06-24" @default.
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• W2019935314 date "2007-03-01" @default.
• W2019935314 modified "2023-09-26" @default.
• W2019935314 title "Kinking the Coiled Coil – Negatively Charged Residues at the Coiled-coil Interface" @default.
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• W2019935314 doi "https://doi.org/10.1016/j.jmb.2006.11.083" @default.
• W2019935314 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17207815" @default.
• W2019935314 hasPublicationYear "2007" @default.
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