Modern Methods of Drug Design and Development, a volume in the Methods in Enzymology series highlights new advances in the field with this new volume presenting interesting chapters on a variety of topics, including Recombinant protein purification for structural and kinetic studies, Steady-state kinetic analysis of reversible enzyme inhibitors, Steady-State Enzyme Kinetics, Analysis of enzyme kinetic data using ICEKAT, NMR techniques in drug discovery, Dynamic simulations and pre-steady state kinetics to guide drug discovery, Design and assay of substrate-product analogues for racemases and epimerases, Sensitive high throughput methods to screen for P450 inhibition: A- MI complex forming drugs, and more.
Other chapters cover Sensitive high throughput methods to screen for P450 inhibition: B-Heme loss causing drugs, Discovery and development of inhibitors of acetyltransferase Eis to combat Mycobacterium tuberculosis, Crystallographic fragment screening in academic cancer drug discovery, Fast fragment- and compound-screening pipeline at the Swiss Light Source, Chemical biology, enzymology and drug discovery, PROTACs, Proximity-Induced Pharmacology (PROTACs), and much more.
1. Cover image - p. Cover 2. Title page - p. ii 3. Table of Contents - p. iii 4. List of Illustrations - p. iii 5. List of Tables - p. iii 6. Copyright - p. iii 7. Contributors - p. iii 8. Preface - p. iii 9. Recombinant protein production for structural and kinetic studies: A case study using M. tuberculosis α-methylacyl-CoA racemase (MCR) - p. iii 10. Steady-state kinetic analysis of reversible enzyme inhibitors: A case study on calf intestine alkaline phosphatase - p. iii 11. Non-equilibrium modalities of inhibition: Characterizing irreversible inhibition for the ErbB receptor family members - p. iii 12. Analysis of continuous enzyme kinetic data using ICEKAT - p. iii 13. You get what you screen for: Standards for experimental design and data fitting in drug discovery - p. iii 14. Analysis of enzyme reactions using NMR techniques: A case study with α-methylacyl-CoA racemase (AMACR) - p. iii 15. Crystallographic fragment screening in academic cancer drug discovery - p. iii 16. Fast fragment and compound screening pipeline at the Swiss Light Source - p. iii 17. Fragment-based screening by protein-detected NMR spectroscopy - p. iii 18. Methods for computer-assisted PROTAC design - p. iii 19. High-throughput cytochrome P450 loss and metabolic intermediate complex assays to aid in designing out of CYP3A inactivation - p. iii 20. Discovery and development of inhibitors of acetyltransferase Eis to combat Mycobacterium tuberculosis - p. iii 21. Design and evaluation of substrate–product analog inhibitors for racemases and epimerases utilizing a 1,1-proton transfer mechanism - p. iii 22. Identification and biochemical characterization of small molecule inhibitors of ERK2 that target the D-recruitment site - p. iii 23. Preparing recombinant “Split AEP” for protein labeling - p. iii 24. Mass cytometry as a tool in target validation and drug discovery - p. iii
Modern Methods of Drug Design and Development, a volume in the Methods in Enzymology series highlights new advances in the field with this new volume presenting interesting chapters on a variety of topics, including Recombinant protein purification for structural and kinetic studies, Steady-state kinetic analysis of reversible enzyme inhibitors, Steady-State Enzyme Kinetics, Analysis of enzyme kinetic data using ICEKAT, NMR techniques in drug discovery, Dynamic simulations and pre-steady state kinetics to guide drug discovery, Design and assay of substrate-product analogues for racemases and epimerases, Sensitive high throughput methods to screen for P450 inhibition: A- MI complex forming drugs, and more.
Other chapters cover Sensitive high throughput methods to screen for P450 inhibition: B-Heme loss causing drugs, Discovery and development of inhibitors of acetyltransferase Eis to combat Mycobacterium tuberculosis, Crystallographic fragment screening in academic cancer drug discovery, Fast fragment- and compound-screening pipeline at the Swiss Light Source, Chemical biology, enzymology and drug discovery, PROTACs, Proximity-Induced Pharmacology (PROTACs), and much more.
1. Cover image - p. Cover 2. Title page - p. ii 3. Table of Contents - p. iii 4. List of Illustrations - p. iii 5. List of Tables - p. iii 6. Copyright - p. iii 7. Contributors - p. iii 8. Preface - p. iii 9. Recombinant protein production for structural and kinetic studies: A case study using M. tuberculosis α-methylacyl-CoA racemase (MCR) - p. iii 10. Steady-state kinetic analysis of reversible enzyme inhibitors: A case study on calf intestine alkaline phosphatase - p. iii 11. Non-equilibrium modalities of inhibition: Characterizing irreversible inhibition for the ErbB receptor family members - p. iii 12. Analysis of continuous enzyme kinetic data using ICEKAT - p. iii 13. You get what you screen for: Standards for experimental design and data fitting in drug discovery - p. iii 14. Analysis of enzyme reactions using NMR techniques: A case study with α-methylacyl-CoA racemase (AMACR) - p. iii 15. Crystallographic fragment screening in academic cancer drug discovery - p. iii 16. Fast fragment and compound screening pipeline at the Swiss Light Source - p. iii 17. Fragment-based screening by protein-detected NMR spectroscopy - p. iii 18. Methods for computer-assisted PROTAC design - p. iii 19. High-throughput cytochrome P450 loss and metabolic intermediate complex assays to aid in designing out of CYP3A inactivation - p. iii 20. Discovery and development of inhibitors of acetyltransferase Eis to combat Mycobacterium tuberculosis - p. iii 21. Design and evaluation of substrate–product analog inhibitors for racemases and epimerases utilizing a 1,1-proton transfer mechanism - p. iii 22. Identification and biochemical characterization of small molecule inhibitors of ERK2 that target the D-recruitment site - p. iii 23. Preparing recombinant “Split AEP” for protein labeling - p. iii 24. Mass cytometry as a tool in target validation and drug discovery - p. iii
