Professor Anthony Mittermaier works in the Department of Chemistry, McGill University, Montreal, Canada. Justin Di Trani is an Assistant Professor at the University of Alberta, Department of Biochemistry, Edmonton, Canada

• PART 1: ITC kinetics measurements1. Enzyme kinetics by ITC2. Measuring binding kinetics by ITC3. Analysing ITC kinetic data with AFFinimeter software4. In vivo enzyme kinetics by ITC5. Characterizing enzyme kinetics by 2D-ITC6. Measuring enzyme stability using ITC7. Kinetics of immobilized enzymes8. Enzyme kinetics in crowded solutions9. Kinetics of nanozymes10. Using ITC to characterize enzyme allostery11. Signal amplification in ITC kinetics experiments12. ITC kinetic studies of 6-phytase13. Catalysis of biological substrates of nuclear metallohydrolases14. Alpha-amylase activity and inhibition15. Enzyme stability and activity of psycrophillic enzymes16. Non-MM kinetics of peroxidases and application to industrial wastes17. Kinetics of diphosphohydrolasesPART 2: ITC thermodynamic measurements18. Interpretation of ITC binding curves19. Analysis of ITC binding data using SEDPHAT20. ITC in drug discovery21. ITC in the development of cancer therapeutics22. Mechanisms of aminoglycoside resistance enzymes23. Using ITC to characterize the interactions of natural products with biomolecules24. ITC studies of metalloenzymes25. Enzyme interactions with toxic metals26. Thermodynamics of molecular machines27. Thermodynamics of protein chaperones28. Characterizing protein interactions in apoptosis by ITC29. Using ITC to study ubiquitination30. Thermodynamics of transition state analogs31. Thermodynamics of recombinant enzymes in biotechnology32. Ion Binding to Transport Proteins using ITC33. Urease from Helicobacter pylori, lessons from ITC34. Substrate recognition by Chitinases35. ITC studies of glycoside hydrolases

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Professor Anthony Mittermaier works in the Department of Chemistry, McGill University, Montreal, Canada. Justin Di Trani is an Assistant Professor at the University of Alberta, Department of Biochemistry, Edmonton, Canada

• PART 1: ITC kinetics measurements1. Enzyme kinetics by ITC2. Measuring binding kinetics by ITC3. Analysing ITC kinetic data with AFFinimeter software4. In vivo enzyme kinetics by ITC5. Characterizing enzyme kinetics by 2D-ITC6. Measuring enzyme stability using ITC7. Kinetics of immobilized enzymes8. Enzyme kinetics in crowded solutions9. Kinetics of nanozymes10. Using ITC to characterize enzyme allostery11. Signal amplification in ITC kinetics experiments12. ITC kinetic studies of 6-phytase13. Catalysis of biological substrates of nuclear metallohydrolases14. Alpha-amylase activity and inhibition15. Enzyme stability and activity of psycrophillic enzymes16. Non-MM kinetics of peroxidases and application to industrial wastes17. Kinetics of diphosphohydrolasesPART 2: ITC thermodynamic measurements18. Interpretation of ITC binding curves19. Analysis of ITC binding data using SEDPHAT20. ITC in drug discovery21. ITC in the development of cancer therapeutics22. Mechanisms of aminoglycoside resistance enzymes23. Using ITC to characterize the interactions of natural products with biomolecules24. ITC studies of metalloenzymes25. Enzyme interactions with toxic metals26. Thermodynamics of molecular machines27. Thermodynamics of protein chaperones28. Characterizing protein interactions in apoptosis by ITC29. Using ITC to study ubiquitination30. Thermodynamics of transition state analogs31. Thermodynamics of recombinant enzymes in biotechnology32. Ion Binding to Transport Proteins using ITC33. Urease from Helicobacter pylori, lessons from ITC34. Substrate recognition by Chitinases35. ITC studies of glycoside hydrolases

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Professor Anthony Mittermaier works in the Department of Chemistry, McGill University, Montreal, Canada. Justin Di Trani is an Assistant Professor at the University of Alberta, Department of Biochemistry, Edmonton, Canada

• PART 1: ITC kinetics measurements1. Enzyme kinetics by ITC2. Measuring binding kinetics by ITC3. Analysing ITC kinetic data with AFFinimeter software4. In vivo enzyme kinetics by ITC5. Characterizing enzyme kinetics by 2D-ITC6. Measuring enzyme stability using ITC7. Kinetics of immobilized enzymes8. Enzyme kinetics in crowded solutions9. Kinetics of nanozymes10. Using ITC to characterize enzyme allostery11. Signal amplification in ITC kinetics experiments12. ITC kinetic studies of 6-phytase13. Catalysis of biological substrates of nuclear metallohydrolases14. Alpha-amylase activity and inhibition15. Enzyme stability and activity of psycrophillic enzymes16. Non-MM kinetics of peroxidases and application to industrial wastes17. Kinetics of diphosphohydrolasesPART 2: ITC thermodynamic measurements18. Interpretation of ITC binding curves19. Analysis of ITC binding data using SEDPHAT20. ITC in drug discovery21. ITC in the development of cancer therapeutics22. Mechanisms of aminoglycoside resistance enzymes23. Using ITC to characterize the interactions of natural products with biomolecules24. ITC studies of metalloenzymes25. Enzyme interactions with toxic metals26. Thermodynamics of molecular machines27. Thermodynamics of protein chaperones28. Characterizing protein interactions in apoptosis by ITC29. Using ITC to study ubiquitination30. Thermodynamics of transition state analogs31. Thermodynamics of recombinant enzymes in biotechnology32. Ion Binding to Transport Proteins using ITC33. Urease from Helicobacter pylori, lessons from ITC34. Substrate recognition by Chitinases35. ITC studies of glycoside hydrolases

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