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Biological Chemistry Seminar

Date:
-
Location:
CP-201

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Catherine Denning will be presenting this week's seminar, titled Investigating the Mechanism of Chemical Denaturation by Fluorescence Resonance Energy Transfer (FRET).

Abstract: Chemical denaturation is a common technique in biochemistry to study the dynamics and stability of proteins. Though use of chemical denaturants is fairly routine, there is no consensus among the biochemistry field for how denaturation occurs. The dominating belief is that chemical denaturants, such as urea or guanidinium chloride (GdmCl), work by affecting the solvent accessible surface area (SASA) of the protein that causes it to break down.1 Recently, due to technology advances, it has been shown through computational studies that a dry molten globular (DMG) state is in rapid equilibrium with the native state of the protein when a denaturant is applied to the system.1 This suggests that chemical denaturants actually work via a two-step process. In his article “ Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride”, Jha uses fluorescence resonance energy transfer (FRET) as well as other techniques to confirm results previously found from computational studies. This seminar will focus on the use of FRET to study the proposed two-step mechanism of denaturation by GdmCl.

References:

1. Jha, S.A.; Marqusee, S. Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride.  Proceedings of the National Academy of Sciences. 2014, 111, 4856-4861.

Course Instructor: Dr. Anne-Frances Miller