Title

Investigation of Trehalose on Protein Stability

Presentation Type

Event

Start Date

27-4-2019 9:30 AM

End Date

29-4-2019 10:44 AM

Abstract

Maintaining protein stability is essential in research involving proteins, especially when studying protein activity at extreme pH or temperature. Cosolvents help stabilize proteins in artificial environments by preventing them from forming aggregates. Glycerol, a common cosolvent, alters the solvent and forces a protein into a more compact volume, thus increasing its stability. Trehalose, will greatly increase protein stability, but it seems to stabilize proteins by some mechanism that involves a specific interaction between the cosolvent and the protein based on the need for an equilibration period before full stabilization occurs. We are studying the interaction between trehalose and a thermophilic protein, SsPL to better understand the mechanism by which this sugar acts to stabilize proteins. We have designed and implemented experiments using ITC to quantitatively investigate this interaction.

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Apr 27th, 9:30 AM Apr 29th, 10:44 AM

Investigation of Trehalose on Protein Stability

Maintaining protein stability is essential in research involving proteins, especially when studying protein activity at extreme pH or temperature. Cosolvents help stabilize proteins in artificial environments by preventing them from forming aggregates. Glycerol, a common cosolvent, alters the solvent and forces a protein into a more compact volume, thus increasing its stability. Trehalose, will greatly increase protein stability, but it seems to stabilize proteins by some mechanism that involves a specific interaction between the cosolvent and the protein based on the need for an equilibration period before full stabilization occurs. We are studying the interaction between trehalose and a thermophilic protein, SsPL to better understand the mechanism by which this sugar acts to stabilize proteins. We have designed and implemented experiments using ITC to quantitatively investigate this interaction.