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• W2316055040 abstract "To determine when second- ary structure forms as two chains coalesce to form an a-helical dimer, the folding rates of variants of the coiled coil region of GCN4 were compared. Residues at non-perturbing posi- tions along the exterior length of the helices were substituted one at a time with alanine and glycine to vary helix propensity and therefore her stability. For all variants, the bimolecu- lar folding rate remains largely unchanged; the unfolding rate changes to largely account for the change in stability. Thus, contrary to most folding models, widespread helix is not yet formed at the rate-limiting step in the folding pathway. The high-energy transition state is a collapsed form that contains little if any sec- ondary structure, as suggested for the globular protein cytochrome c (Sosnick et al., Proteins" @default.
• W2316055040 created "2016-06-24" @default.
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• W2316055040 date "1996-01-01" @default.
• W2316055040 modified "2023-09-27" @default.
• W2316055040 title "The Role a-Helical of Helix Formation in the Folding of a Fully Coiled Coil" @default.
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