Application Note

Detecting Protein Conformational Change Due to Ligand Binding and Stabilization Using MMS

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Application Note

This Application Note Highlights:

  • Protein was tested with two different ligands: one that completely stabilizes the protein against heat stress, and the other that moderately stabilizes it against heat stress.
  • Determining of the secondary structure of proteins with and without ligands, offering  a more complete understanding of how the ligand alters the protein’s function
  • Modulating between sample and reference buffer with the flow cell utilized by  The AQS3pro 
  • Enabling realtime, highly accurate and compatable buffer subtraction with MMS,  for use with any ligand.

Detecting Protein Conformational Change

Ligand binding can affect the function of proteins and often causes protein conformational change. Since form fits function, determining the secondary structure of proteins with and without ligands is essential for a more complete understanding of how the ligand alters the protein’s function. RedShiftBio has developed a new technology called Microfluidic Modulation Spectroscopy (MMS) that measures protein secondary structure by combining infrared spectroscopy with microfluidics to enhance sensitivity and accuracy.

Change How You See Biomolecules

Microfluidic Modulation Spectroscopy provides a powerful alternative, producing consistently reproducible data that goes beyond that supplied by current techniques. The high-performance fully automated AQS3pro system and AQS3delta analytics package allow scientists to quickly and easily run samples, process data and gain insight.

AQS3pro

Next generation in protein structure determination.

The AQS³pro powered by Microfluidic Modulation Spectroscopy is the next generation infrared based spectroscopy platform for protein structure determination. It represents a novel tool that will strengthen you bioanalytical tool kit and provide critical insights into protein based drug development.
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