The structure of the protein folding transition state ensemble is traditionally inferred from changes in both thermodynamic and kinetic properties of the protein in question through side-chain mutations.  However, this method does not offer direct information regarding the dynamics of backbone-backbone hydrogen bond (BB-HB) formation, an important energetic and structural feature of proteins.  Here, we show our efforts to modulate BB-HB strengths via thioamide mutations to site-specifically study individual hydrogen bond contributions to protein folding.  To demonstrate this technique, we examine the intramolecular BB-HB network of a variant of the well-studied tryptophan zipper (Trpzip) and the extent of hydrogen bond formation in its folding transition state.

Site-specifically probing backbone-backbone hydrogen bond formation in the folding transition state of beta-sheet proteins

244th National Meeting (2012)

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