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Printable Handouts
Navigable Slide Index
- Introduction
- Research questions
- Dihydrofolate reductase
- Dihydrofolate reductase reaction and structure
- Kinetic scheme of DHFR catalysis
- DHFR structures (Swaya and Kraut)
- Hydride transfer rates data
- DHFR chain
- Are the mutations coupled or not coupled?
- Triple mutant cycle
- Long range coupling interactions in DHFR
- Hydride transfer reaction
- NADPH binding affinity
- DHFR dynamics by NMR spectroscopy
- Energy landscape of catalysis
- Coupled loop motions in DHFR
- Network of coupled motions in DHFR
- Link between motions and catalysis
- Time-resolved conformational changes
- Conformational changes vs. enzymatic reaction
- Protein motions occur on many timescales
- Adenylate kinase' relevant states at equilibrium
- Fast motion hypothesis
- Role of electrostatic interactions in catalysis
- Vibrational spectroscopy for electrostatics
- Thiocyanate probe
- Electrostatics in DHFR
- Electrostatic landscape of enzyme catalysis
- Electrostatic reorganization in DHFR
- Frequency and field related by stark tuning rate
- Decomposition of electric field contributions
- Conformation – electrostatics – catalysis
- Major contributors to the electric field
- Summary
- Acknowledgments
Topics Covered
- How do enzyme motions and fluctuations impact catalysis?
- Are the times scales for protein structural changes and the enzymatic catalytic cycle similar?
- How are electrostatics modulated in enzyme active sites in conjunction with catalysis?
- Dihydrofolate reductase as a model: kinetics, reactions & structure
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Talk Citation
Benkovic, S. (2017, July 31). Perspectives on biological catalysis [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved January 24, 2021, from https://hstalks.com/bs/43/.Publication History
Financial Disclosures
- Prof. Stephen Benkovic has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.