An Antiparallel α-Helical Coiled-Coil Model System for Rapid Assessment of Side-Chain Recognition at the Hydrophobic Interface
Journal of the American Chemical Society2006Vol. 128(51), pp. 16444–16445
Citations Over TimeTop 13% of 2006 papers
Abstract
Both parallel and antiparallel alpha-helical coiled-coil dimers are common among proteins; however, biophysical scrutiny has focused almost entirely on parallel dimers. We describe the development of a model system that enables efficient and systematic analysis of hydrophobic packing between antiparallel alpha-helices. Our findings reveal significant differences in packing preferences between parallel and antiparallel coiled-coils.
Related Papers
- → A Set of Computationally Designed Orthogonal Antiparallel Homodimers that Expands the Synthetic Coiled-Coil Toolkit(2014)64 cited
- → Antiparallel Four-Stranded Coiled Coil Specified by a 3-3-1 Hydrophobic Heptad Repeat(2006)60 cited
- → Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection(2016)20 cited
- → Structure of a truncated form of leucine zipper II of JIP3 reveals an unexpected antiparallel coiled-coil arrangement(2016)8 cited
- → Design and stability of a novel coiled-coil peptide(2006)1 cited