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Solvation in protein (un)folding: Effect of local and bulk dynamics in the melittin tetramer-monomer transition
Proceedings of the National Academy of Sciences (2009)
  • Christina M Othon, Wesleyan University
  • Oh-Hoon Kwon, California Institute of Technology
  • Milo M Lin, California Institute of Technology
  • Ahmed H Zewail, California Institute of Technology
Abstract

Protein structural integrity and flexibility are intimately tied to solvation. Here we examine the effect that changes in bulk and local solvent properties have on protein structure and stability. We observe the change in solvation of an unfolding of the protein model, melittin, in the presence of a denaturant, trifluoroethanol. The peptide system displays a well defined transition in that the tetramer unfolds without disrupting the secondary or tertiary structure. In the absence of local structural perturbation, we are able to reveal exclusively the role of solvation dynamics in protein structure stabilization and the (un)folding pathway. A sudden retardation in solvent dynamics, which is coupled to the change in protein structure, is observed at a critical trifluoroethanol concentration. The large amplitude conformational changes are regulated by the local solvent hydrophobicity and bulk solvent viscosity.

Publication Date
Spring May 29, 2009
Citation Information
Christina M Othon, Oh-Hoon Kwon, Milo M Lin and Ahmed H Zewail. "Solvation in protein (un)folding: Effect of local and bulk dynamics in the melittin tetramer-monomer transition" Proceedings of the National Academy of Sciences Vol. 106 Iss. 31 (2009)
Available at: http://works.bepress.com/christina_othon/4/