English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The objective of this study was to investigate the positional effect of hydrophobic interactions in the alpha-helical interface in controlling the formation of two-stranded and four-stranded coiled-coils. Two disulfide-bridged antiparallel coiled-coils were designed which differ only in the position of a single Ala residue in the middle heptad: in peptide 2H the Ala residues are in register (in the same rung), while in peptide 4H they are not. Data from size-exclusion chromatography and sedimentation equilibrium experiments showed that under benign conditions peptides 2H and 4H were two-stranded and four-stranded coiled-coils respectively. These results, in conjunction with molecular modeling studies, suggests that when four Ala residues are in the same plane of a potential four-stranded coiled-coil, the small side chains of Ala would create a large cavity in the hydrophobic interface of the potential four-stranded structure which is destabilizing and favors the two-stranded, disulfide-bridged coiled-coil. In contrast, an alternating Leu-Ala hydrophobic packing in the two planes distributes the potential cavity over a larger region, which may be partially filled by minor adjustments of the neighboring Leu side chains. As a result, there is still sufficient hydrophobic contact to maintain the four stranded structure.

The relative positions of alanine residues in the hydrophobic core control the formation of two-stranded or four-stranded α-helical coiled-coils