The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function.

ABSTRACT: The protein folding problem is often studied by comparing the mechanisms of proteins sharing the same structure but different sequence. The recent design of the two proteins G(A)88 and G(B)88, displaying different structures and functions while sharing 88% sequence identity (49 out of 56 amino acids), allows the unique opportunity for a complementary approach. At which stage of its folding pathway does a protein commit to a given topology? Which residues are crucial in directing folding mechanisms to a given structure? By using a combination of biophysical and computational techniques, we have characterized the folding of both G(A)88 and G(B)88. We show that, contrary to expectation, G(B)88, characterized by a native α+β fold, displays in the denatured state a content of native-like helica

SUBMITTER: Morrone A 

PROVIDER: S-EPMC3030387 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature