Three topologically equivalent core residues affect the transition state ensemble in a protein folding reaction.

Abstract excerpt

The single domain protein, interleukin-1beta, is representative of a distinct class of proteins characterized by their beta-trefoil topology. Each subdomain of this structural class is composed of a beta beta beta loop beta (betabetabetaLbeta) motif comprised of approximately 50 residues and gives the protein a pseudo- 3-fold axis of symmetry. A common feature of proteins in this topological family appears to be...

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