771490-16-5Relevant articles and documents
Side-chain pairing preferences in the parallel coiled-coil dimer motif: Insight on ion pairing between core and flanking sites
Steinkruger, Jay D.,Woolfson, Derek N.,Gellman, Samuel H.
supporting information; experimental part, p. 7586 - 7588 (2010/07/09)
A new strategy for rapid evaluation of sequence-stability relationships in the parallel coiled-coil motif is described. The experimental design relies upon thiol-thioester exchange equilibria, an approach that is particularly well suited to examination of heterodimeric systems. Our model system has been benchmarked by demonstrating that it can quantitatively reproduce previously reported trends in interhelical a-a′ side-chain pairing preferences at the coiled-coil interface. This new tool has been used to explore the role of Coulombic interactions between a core position on one helix and a flanking position on the other helix (a-g′). This type of interhelical contact has received relatively little attention to date. Our results indicate that such interactions can influence coiled-coil partner preferences.
An antiparallel α-helical coiled-coil model system for rapid assessment of side-chain recognition at the hydrophobic interface
Hadley, Erik B.,Gellman, Samuel H.
, p. 16444 - 16445 (2007/10/03)
Both parallel and antiparallel α-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 α-helices. Our findings reveal significant differences in packing preferences between parallel and antiparallel coiled-coils. Copyright
