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170 2004 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim DOI: 10.1002/cbic.200300781 ChemBioChem 2004, 5, 170 176 Coiled Coil Domains: Stability, Specificity, and
 

Summary: 170 ¹ 2004 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim DOI: 10.1002/cbic.200300781 ChemBioChem 2004, 5, 170 ±176
Coiled Coil Domains: Stability, Specificity, and
Biological Implications
Jody M. Mason and Katja M. Arndt*[a]
Introduction
The coiled coil is a common structural motif,
formed by approximately 3 ± 5% of all amino
acids in proteins.[1]
Typically, it consists of two to
five a-helices wrapped around each other into a
left-handed helix to form a supercoil. Whereas
regular a-helices go through 3.6 residues for
each complete turn of the helix, the distortion
imposed upon each helix within a left-handed
coiled coil lowers this value to around 3.5. Thus
a heptad repeat occurs every two turns of the
helix.[2, 3]
The coiled coil was first described by
Crick in 1953.[4]
He noted that a-helices pack

  

Source: Arndt, Katja - Institut für Biologie III, Albert-Ludwigs-Universität Freiburg
Mason, Jody - Department of Biological Sciences, University of Essex

 

Collections: Biology and Medicine; Biotechnology