NDLI: Improving coiled-coil stability by optimizing ionic interactions.

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Improving coiled-coil stability by optimizing ionic interactions.

Content Provider	Semantic Scholar
Author	Burkhard, Peter Ivaninskii, Sergei Lustig, Ariel
Copyright Year	2002
Abstract	Alpha-helical coiled coils are a common protein oligomerization motif stabilized mainly by hydrophobic interactions occurring along the coiled-coil interface. We have recently designed and solved the structure of a two-heptad repeat coiled-coil peptide that is stabilized further by a complex network of inter- and intrahelical salt-bridges in addition to the hydrophobic interactions. Here, we extend and improve the de novo design of this two heptad-repeat peptide by four newly designed peptides characterized by different types of ionic interactions. The contribution of these different types of ionic interactions to coiled-coil stability are analyzed by CD spectroscopy and analytical ultracentrifugation. We show that all peptides are highly alpha-helical and two of them are 100% dimeric under physiological conditions. Furthermore, we have solved the X-ray structure of the most stable of these peptides and the rational design principles are verified by comparing this structure to the structure of the parent peptide. We show that by combining the most favorable inter- and intrahelical salt-bridge arrangements it is possible to design coiled-coil oligomerization domains with improved stability properties.
Starting Page	599
Ending Page	603
Page Count	5
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://hasyweb.desy.de/science/annual_reports/2001_report/part2/contrib/72/5203.pdf
PubMed reference number	12054832v1
Volume Number	318
Issue Number	3
Journal	Journal of molecular biology
Language	English
Access Restriction	Open
Subject Keyword	Analytical Ultracentrifugation Coil Device Component Coiled-Coil Domain Protein Domain protein oligomerization
Content Type	Text
Resource Type	Article

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