Using loop length variants to dissect the folding pathway of a four-helix-bundle protein.

Abstract excerpt

Rop is a four-helix-bundle protein formed by the association of two helix-loop-helix monomers. The short helix-connecting loop was replaced with a series of polyglycine linkers of increasing length. These mutant proteins all appear to fold via the same general mechanism as that of the wild-type protein, even at the longest loop lengths. Replacement of the wild-type two-residue loop (Asp-Ala) with a (Gly-Gly)...

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