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- W4062319 endingPage "70" @default.
- W4062319 startingPage "35" @default.
- W4062319 abstract "Coiled coil motifs are, despite their apparent simplicity, highly specific, and play a significant role in the understanding of tertiary structure and its formation. The most commonly observed of the coiled coils, the parallel dimeric, is yet to be fully characterized for this structural class in general. Nonetheless, strict rules have emerged for the necessity of specific types of amino acids at specific positions. In this chapter, we discuss this system in light of existing coiled coil structures and in applying rules to coiled coils that are to be designed or optimized. Understanding and expanding on these rules is crucial in using these motifs, which play key roles in virtually every cellular process, to act as drug-delivery agents by sequestering other proteins that are not behaving natively or that have been upregulated (for example, by binding to coiled coil domains implicated in oncogenesis). The roles of the a and d hydrophobic core positions and the e and g electrostatic edge positions in directing oligomerization and pairing specificity are discussed. Also discussed is the role of these positions in concert with the b, c, and f positions in maintaining alpha-helical propensity, helix solubility, and dimer stability." @default.
- W4062319 created "2016-06-24" @default.
- W4062319 creator A5004541105 @default.
- W4062319 creator A5013810790 @default.
- W4062319 creator A5087515137 @default.
- W4062319 date "2006-10-14" @default.
- W4062319 modified "2023-09-23" @default.
- W4062319 title "Considerations in the Design and Optimization of Coiled Coil Structures" @default.
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