Effects of Trifluoroethanol on the Stability and Folding Dynamics on SH3 and ACBP

Effects of Trifluoroethanol on the Stability and Folding Dynamics on SH3 and ACBP

Document Type

Abstract

Publication Date

10-2-2019

Abstract

Protein folding is a complicated process that is typically determined by complex energy landscapes that can be altered by outside factors like temperature, mutation, or the chemical environment surrounding the proteins. Trifluoroethanol or TFE is an organic, colorless, water-miscible alcohol that is used in various chemical, pharmaceutical, and engineering applications. TFE is known for stabilizing protein secondary structure specifically, alpha-helical conformations. Denaturation melts involving TFE were tested on Acyl CoA binding protein, (ACBP) and SH3 protein due to their difference in native secondary structures; ACBP is comprised of mainly alpha helices and SH3 is comprised of mainly beta sheets. These experiments reveal that TFE has a large impact on the thermodynamics of both proteins and possibly leads to a change in the conformation or folding pathways of the two proteins tested.

Project Mentor

Prof. E. Guinn, PhD

Funding and Acknowledgements

Funding: Merck/James S. MacDonald Summer Stipend

Effects of Trifluoroethanol on the Stability and Folding Dynamics on SH3 and ACBP

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