MSF

MSF characterizes nonreversible thermal unfolding of proteins by generating nonreversibility curves from modulated temperature cycles and determining the onset temperature (T_nr) to assess protein stability.

Key Features:

• Microvolume Sample Analysis: Operates on as little as 10 µL of sample volume, requiring only a few micrograms of protein.
• Incremental Temperature Cycles: Performs incremental/modulated temperature cycles to derive nonreversibility curves of thermal protein unfolding and determine the onset temperature (T_nr) for irreversible unfolding.
• Compatibility with Existing Technology: Builds upon the hardware foundation of nanoDSF technology, enabling simultaneous analysis of multiple samples.

Scientific Applications:

• pH Influence on Protein Stability: Investigates how solution pH affects the reversibility of thermal protein unfolding across model proteins and provides T_nr as a biophysical parameter distinct from traditional thermal denaturation data.
• Enzyme Stability Studies: Examines enzyme stability following exposure to elevated temperatures to characterize irreversible unfolding behavior.
• Impact of Protein Modifications: Assesses how modifications such as PEGylation and fluorescent dye labeling influence thermal unfolding and nonreversibility.
• Protein Interaction Effects: Studies how different protein interactions impact the reversibility of thermal unfolding.

Methodology:

Uses modulated/incremental temperature cycles to generate nonreversibility curves, which are analyzed to identify the onset temperature for irreversible unfolding (T_nr).