1. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Green Chemistry
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Why use biocatalysis? Green chemistry & Catalytic power of enzymes
Why proteins need engineering: stability, optimization for new substrate, new metabolic pathways |
![URL](/home/images/search/btnUrl.gif) |
2. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Enzyme Stability
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Measuring Enzyme Enantioselectivity - stereoisomers, enantiomers, kinetic resolution, asymmetric synthesis, pharmaceutical intermediates
Measuring Enzyme Enantioselectivity and Rates - Michaelis-Menten Kinetics, kinetic resolution, asymmetric synthesis, other metrics to measure rate |
![URL](/home/images/search/btnUrl.gif) |
3. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Enzyme Stability, Selectivity
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Looking at protein structures - protein data bank, Pymol, lactate dehydrogenase
Rational design of more stable enzymes - entropy, hydrophobic effect, helix capping, molten globule |
![URL](/home/images/search/btnUrl.gif) |
4. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Enzyme Selectivity
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Improving selectivity by rational design - intermolecular forces, changing substrate specificity, enantioselectivity mechanisms
Designing faster enzymes - diffusion limit, transition state stabilization, perhydrolysis |
![URL](/home/images/search/btnUrl.gif) |
5. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Enzyme Selectivity
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Designing faster enzymes, pt 2 - chorimate mutase, triosphosphate isomerase, weak binding of substrate.
Computer modeling: molecular mechanics - multiple properties, qualitative design, force fields, atom types |
![URL](/home/images/search/btnUrl.gif) |
6. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Engineering Selectivity
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Enzyme modeling using molecular mechanics - Amber, MM2, FoldX
Modeling to predict protein improvement - stability, molecular dynamics, QM/MM methods |
![URL](/home/images/search/btnUrl.gif) |
7. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Circular Permutation /Selectivity
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Guest lecture (tentative)
Modeling to predict protein improvement - enantioselectivity, bioinformatics, consensus sequence |
![URL](/home/images/search/btnUrl.gif) |
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![문서 문서](/home/images/search/ico_pdf.gif) |
Circular Permutation /Selectivity
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Guest lecture (tentative)
Modeling to predict protein improvement - enantioselectivity, bioinformatics, consensus sequence |
![URL](/home/images/search/btnUrl.gif) |
8. |
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Exam 1 |
Exam 1 |
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9. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Design faster enzymes
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1. Overview of directed evolution: screening, random mutagenesis
2. Mutagenesis using error prone PCR - methods, polymerase fidelity
3. Mutagenesis using error prone PCR - limitations, codon redundancy |
![URL](/home/images/search/btnUrl.gif) |
10. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Mutagenesis Single Substitution
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1. Mutagenesis using recombination methods - chimeras & DNA shuffling,
2. Mutagenesis using recombination methods - limitations, homology
3. Mutagenesis using recombination methods - alternative methods, non-homologous recombination, |
![URL](/home/images/search/btnUrl.gif) |
11. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Multiple Substitutions
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1. Focused substitutions at a single site, saturation mutagenesis methods, degenerate codons
2. Focused substitutions at a single site, choosing locations for mutagenesis
Combining substitutions at multiple sites, stepwise approaches |
![URL](/home/images/search/btnUrl.gif) |
12. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Recombination Methods
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Combining substitutions at multiple sites, simultaneous, reduced amino acid sets
Other mutagenesis approaches insertions, deletions, circular permutations |
![URL](/home/images/search/btnUrl.gif) |
13. |
![문서 문서](/home/images/search/ico_pdf.gif) |
Screening
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Neutral drift libraries - evolutionary justification
Incorporating unnatural amino acids, stop codon translation, substitutions using by feeding auxotrophic strains |
![URL](/home/images/search/btnUrl.gif) |
14. |
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in class presentations |
in class presentations |
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15. |
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Exam 2 |
Exam 2 |
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