Abstract
| Original language | English |
|---|---|
| Title of host publication | Protein Engineering Protocols |
| Editors | K. M. Arndt, K. M. Muller |
| Publisher | Humana Press |
| Pages | 35-70 |
| ISBN (Print) | 9781588290724 |
| DOIs | |
| Publication status | Published - 2007 |
Publication series
| Name | Methods in Molecular Biology |
|---|---|
| Volume | 352 |
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Considerations in the design and optimization of coiled coil structures. / Mason, Jody M.; Muller, Kristian M.; Arndt, Katja M.
Protein Engineering Protocols. ed. / K. M. Arndt; K. M. Muller. Humana Press, 2007. p. 35-70 (Methods in Molecular Biology; Vol. 352).Research output: Chapter in Book/Report/Conference proceeding › Chapter
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TY - CHAP
T1 - Considerations in the design and optimization of coiled coil structures
AU - Mason, Jody M.
AU - Muller, Kristian M.
AU - Arndt, Katja M.
PY - 2007
Y1 - 2007
N2 - 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 α-helical propensity, helix solubility, and dimer stability.
AB - 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 α-helical propensity, helix solubility, and dimer stability.
UR - http://dx.doi.org/10.1385/1-59745-187-8:35
U2 - 10.1385/1-59745-187-8:35
DO - 10.1385/1-59745-187-8:35
M3 - Chapter
SN - 9781588290724
T3 - Methods in Molecular Biology
SP - 35
EP - 70
BT - Protein Engineering Protocols
A2 - Arndt, K. M.
A2 - Muller, K. M.
PB - Humana Press
ER -