Steve Ealick's Research Group
1YMR, Y92A mutant
1YMW, Y92G mutant
1YMN, Y92L mutant
*2OP2, double-mutant (V43C R85C) with extra disulfide bond
This work consisted of studying the reductive unfolding pathways of bovine pancreatic ribonuclease. The atomic coordinates of the refined RNase A structure (PDB access code: 1JVU) were used to determine the structure of the mutants by molecular replacement. Analysis of the structures as well as data about thermodynamic, and reductive unfolding properties, shows that a single intramolecular interaction is responsible for the heterogeneity in the reductive unfolding pathways of ribonuclease A.
The crystallographic asymmetric unit consists of one polypeptide chain.
Xu G, Narayan M, Kurinov I, Ripoll DR, Welker E, Khalili M, Ealick SE, and Scheraga HA. A Localized Specific Interaction Alters the Unfolding Pathways of Structural Homologues. J. Am. Chem. Soc. 128:1204-1213 (2006).
Pradeep, L, Kurinov, I, Ealick, SE, and Scheraga, HA. Implementation of a k/k0 Method to Identify Long-Range Structure in Transition States during Conformational Folding/Unfolding of Proteins. Structure 15:1178-89 (2007).