157. Enzymes & Their Inhibitors

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157. Enzymes & Their Inhibitors

 

 

CATEGORY: Diet Nutrition Supplementation – 500 Courses

COURSE NUMBER: 157

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Syllabus

1.1 Introduction
1.2 Primary Structure
1.2.1 Van der Waals Interactions
1.2.2 Hydrogen and Ionic Bonds
1.2.3 Hydrophobic Interactions
1.2.4 Peptide Bonds
1.3 Secondary Structure
1.3.1 Torsion Angles.
1.3.2 Ramachandran Plot
1.3.3 a-Helixes
1.3.4 b-Sheets
1.3.5 Reverse Turns and Loops
1.3.6 Prediction of a-Helixes, b-Sheets, and Reverse Turns in Peptide
Sequences
1.3.7 Prediction of the Hydropathy or Polarity of Peptide Sequences
1.4 Folding of the Protein into Specific Conformations.
1.4.1 Tertiary Structure
1.4.2 Quaternary Structure
1.5 Posttranslational Modification
1.6 Structural Classification
1.7 Enzyme Classification by Function
1.8 Enzymes and Active Sites
1.8.1 Cofactors
1.8.2 Enzyme Interactions with Substrates and Cofactors
1.8.3 Tyrosyl tRNA Synthetase
1.8.4 Human Aldose Reductase
1.8.5 Dihydropteroate Synthase
1.8.6 DOPA Decarboxylase
1.9 Measurement of Enzyme Ligand Interactions
1.9.1. Independent Binding Sites
1.9.2 Allosteric Behavior — Homotropic Interactions.
1.9.3 Allosteric Interactions between Two Different Ligands —
Heterotropic Interactions

1.10 Specificity, Protein Engineering, and Drug Design
Acknowledgments
Bibliography

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