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]
About the author asgharrazavi
Asghar Razavi is a postdoctoral associate at the Department of Physiology and Biophysics at Weill Cornell Medical College of Cornell University. He received his Ph.D. in Computational Chemistry and Biophysics from Temple University, Philadelphia, USA. His current research at the Weinstein lab focuses on developing molecular level quantitative kinetic models to understand thermodynamics, kinetics, and conformational pathways during function of neurotransmitter transporters and G protein-coupled receptors.
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June 23, 2017
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January 7, 2017
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Dopamine Transporter