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Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology
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Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

DOI:
10.3791/63495-v

•

09:39 min

•

March 31, 2022

•

, , , ,
1The Azrieli Faculty of Medicine in the Galilee,Bar-Ilan University, 2Asian Liver Center, Department of Surgery,Stanford University School of Medicine

章

  • 00:04Introduction
  • 01:16Chip Activation
  • 02:09Target Protein Immobilization
  • 03:09Preparing Analyte Samples and Running the Experiment
  • 06:09Analysis
  • 06:43Results: Data Files Generated from Hsp90 and Cdc37 Interaction Using FEB System (Experiment 1 and 2) and ITC Analysis
  • 08:39Conclusion

概要

自動翻訳

自動翻訳

Field-effect biosensing (FEB) is a label-free technique for detecting biomolecular interactions. It measures the electric current through the graphene biosensor to which the binding targets are immobilized. The FEB technology was used to evaluate biomolecular interactions between Hsp90 and Cdc37 and a strong interaction between the two proteins was detected.

タグ

Biomolecular InteractionMolecular Chaperone Hsp90Client Protein Kinase Cdc37Field-effect Biosensing TechnologyFEBLabel-freeCost-effectiveInteraction DetectionInhibitor TestingAutomatedUser-friendlyPharmaceuticalsBiomolecular AnalysisDrug ValidationChip FunctionalizationEDCSulfo-NHSMES BufferPBSTarget MoleculeQuench Solution

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