Experimental research has shown that the stability of the C-terminal hairpin of Protein G (GB1) increases with the number of tryptophan (Trp) residues. However, the increase in Trp residues also increase the folding time. To understand the roots of this behavior we performed extensive explicit water molecular dynamic (MD) simulations (~10 milliseconds total) on the GB1 hairpin and its Trp zipper mutants.
- Journal article: Kinetic network models of tryptophan mutations in β-hairpins reveal the importance of non-native interactions, Asghar M. Razavi and Vincent A. Voelz, Journal of Chemical Theory and Computation 11: 2801-2812, 2015
- Poster: Razavi, A. M., & Voelz, V. A. (2015, February). Kinetic network models of tryptophan mutations in β-hairpins reveal the importance of non-native interactions. Poster presented at the Biophysical Society 59th Annual Meeting, Baltimore, MD. [PDF]