Denatured State Conformational BIAS in a 3-Helix Bundle

Abstract

Previous work with the four-helix bundle protein cytochrome c' from Rhodopseudomonas palustris using histidine-heme loop formation thermodynamic methods revealed fold-specific deviations from random coil behavior in its denatured state ensemble. To examine the generality of this finding, we extend this work to a three-helix bundle polypeptide, the second ubiquitin