Unique Role of Clusters of Electrostatic Attractions in Controlling the Stability of Two-stranded α-Helical Coiled-Coils
A major goal of protein research is to relate amino acid sequence to protein structure and function. Describing all inter-residue interactions that contribute to the threshold stability required to initiate protein folding is key to achieving this end. The two-stranded α-helical coiled-coil is a simplified protein motif well suited for studying these interactions. Our laboratory has shown that clusters of stabilizing and destabilizing residues in the hydrophobic core control coiled-coil stability [1, 2]. We have also shown that the effect of chain length on coiled-coil stability depends on the composition of the added/removed heptads . Here we investigate the existence of stabilizing sequence electrostatic-clusters and whether they trigger folding and confer final stability, or confer final stability without governing folding.
Results and Discussion
KeywordsPolypeptide Chain Hydrophobic Core Final Stability Native Sequence Alanine Residue
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