| 1. | |
강의소개 |  |
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| 2. | |
단백질의 구성요소 | 1. Protein의 기능 및 역할 2. Protein Source 3. Protein의 구성요소 4. a-Amino Acid 5. The Stereochemistry of Amino Acids 6. pH and pKa 7. Zwitterionic Form 8. Net Charge of Amino Acids 9. Isoelectric Point (pI) 10. Calculation of pI value 11. Negatively Charged R Groups 12. Amino Acids (Acids and Amides) | |
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아미노산의 물리화학적 특성 | 1. Positively Charged R Groups 2. Histidine(Acid/Base Activity) 3. Amino Acids(Alcohols) 4. Amino Acids(Sulfur) 5. Polar (Hydrophilic) R Groups 6. Aliphatic Amino Acids 7. Proline 8. Aromatic Amino Acids 9. Absorption at 280nm 10. Nonpolar (Hydrophobic) R Groups 11. The 20 Amino Acids 12. Peptide Bond | |
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| 3. | |
Intermolecular Forces | 1. The Central Dogma 2. Protein Folding 3. Attractive and Repulsive Forces 4. van der Waals Interaction 5. Hydrogen Bonds 6. Covalent Bond Length 7. Ionic Bonding 8. Ionic Interaction 9. Intermolecular Forces 10. Hydrophobic Interaction 11. Disulfide Bond 12. Covalent Bond Energy 13. Interaction Types in Protein Folding | |
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Protein Structures | 1. Protein Structure 2. Alpha Helix 3. Beta Sheet 4. Random Coil 5. Protein Motif 6. Helix-turn-helix Motif 7. Helix-loop-helix Motif 8. Coiled-Coil Motif 9. Leucine Zipper Motif 10. Zinc Finger Motif 11. Beta Hairpin Motif 12. Greek Key Motif 13. Beta-Barrel Structure 14. Protein Folding 15. Recombinant Protein As Inclusion Body 16. Denaturation of Misfolded Protein 17. Protein Refolding Technology | |
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| 4. | |
Recombinant Proteins | 1. Enzyme Activity 2. Recombinant DNA Technology 3. Expression of Recombinant Proteins 4. Overexpression of Recombinant Proteins 5. Crystals of Recombinant Protein 6. Engineering Proteins for Ease of Purification 7. Process of Protein Purification 8. 효소 단백질의 안정화 조건 9. 효소 단백질의 안정화제 10. Methods for Total Protein Determination 11. UV Absorbance of DNA and Protein 12. Bradford Assay 13. Interfering Compounds for Assays to Quantitate | |
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Downstream Processing | 1. Upstream Process for the Recombinant Proteins 2. Downstream Process for the Recombinant Proteins 3. Differences between Upstream and Downstream Processes 4. SDS-Poly Acrylamide Gel Electrophoresis 5. Two-Dimensional Gel Electrophoresis 6. Methods for Protein Purification 7. Processes of Protein Purification 8. Protein Purification 9. Required Purity of Biotechnology Products 10. Process Costs | |
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| 5. | |
비기계적 세포파쇄법 | 1. Recovery of Intracellular Proteins 2. Host Cells for Proteins 3. Bacterial Cell Walls 4. Gram-Positive Bacteria 5. Gram-Negative Bacteria 6. Cell Wall of Fungi 7. Fungi: Yeast and Mould 8. Plant Cell Wall 9. Mammalian Cell Wall 10. 비기계적인 세포파쇄법 (Nonmechanical Cell Disruption) 11. Cell Disruption with Detergents 12. Cell Disruption with Organic Solvents 13. Cell Disruption with Enzymes 14. Cell Disruption by Osmotic Shock | |
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기계적 세포파쇄법 | 1. 기계적인 세포파쇄법 (Mechanical Cell Disruption) 2. Homogenizer 3. Blender 4. Sonicator 5. Ultrasonic Cell Disruption 6. Zirconia-silica Beads (0.5mm) 7. Bead Mill Operation 8. High-Pressure Homogenization 9. Impinging-Jet Fluidizer 10. Efficiency of Cell Disrupt Methods 11. Possible Damages of Protein after Cell Disruption | |
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| 6. | |
Centrifugation | 1. Recovery of Intracellular Proteins 2. Factors Affecting in Centrifugation 3. Densities of Cell Particles 4. Forces in Centrifugation 5. Sedimentation Coefficient 6. Relative Centrifugal Force (RCF) 7. Centrifuge Speed 8. Centrifuge Classes 9. Centrifuge Types 10. Differential Centrifugation 11. Isopycnic Gradients 12. Safety Aspects in Centrifugation | |
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Filtration | 1. Dead-end/Cross-flow Filtration 2. Depth Filtration 3. Depth Filter Materials 4. Filter Press 5. Rotary Vacuum Filtration 6. Absolute (Membrane) Filteration 7. Membrane Filter Materials 8. Comparison of Membrane Filtration 9. Filtration Selection 10. Diafiltration 11. Causes of Membrane Fouling 12. Prevention of Membrane Fouling 13. Types of Fouling and Chemical Treatments | |
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| 7. | |
Salting in and Salting out | 1. Protein Subcellular Localization 2. Transmembrane Proteins 3. Membrane Proteins 4. Protein Insolubility 5. Salting in (Solubility) 6. Chaotropic Ions 7. Additives for Salting in 8. Salting out (Precipitation) 9. Kosmotropic Ions 10. Additives for Salting out 11. Ammonium Sulfate, (NH4)2SO4 | |
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Membrane Protein Solubility | 1. 막 단백질의 용해 방법 2. Membrane Protein Solubility 3. Membrane Protein Solubility 4. Anionic (SDS) and Nonionic (Triton X-100) Detergents 5. Critical Micelle Concentration (CMC) 6. Comparison of Detergents 7. Membrane Protein Solubility | |
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| 8. | |
Protein concentration | 1. 단백질 용액의 농축 2. Agents To Precipitate Proteins 3. Ammonium Sulfate in Buffer Solution Adsorbs Waters from Protein Solution 4. 단백질의 분별침전 5. 염석(salting out)에 의한 단백질 분별침전 6. 유기용매에 의한 단백질 분별침전 7. pH에 의한 단백질 분별침전 8. 수용성폴리머에 의한 단백질 분별침전 9. 단백질 용액의 농축 10. 원심식 한외거르기막 11. 이방성막 농축장치 12. 막관다발 (Hollow fiber) | |
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Removing salts | 1. 단백질 용액의 농축 2. 동결건조기 3. Swelling Factor (ml/g) of Gel Type 4. 탈염 (Removing Salts) | |
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| 9. | |
Aqueous Two-Phase (Polymer/Salt) Systems | 1. Aqueous Two-Phase System 2. Binodial Curve and Tie Line 3. Example of PEG/Salt Two-Phase systems 4. 수성이상계 – 단백질 정량 체크 5. 수성이상계 기질활성체크 6. PEG/SALT SYSTEMS 7. Factors Affecting in Aqueous Two Phase System 8. The Partition Coefficient (K) 9. The Purification Factor (PF) 10. Recovery Enzymatic Activity 11. Aqueous Two-Phase System | |
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Aqueous Two-Phase (Polymer/Polymer) Systems | 1. Aqueous Partitioning 2. Aqueous Two-Phase (Polymer/Polymer) Systems 3. 폴리머 용액의 조제법 4. PEG-DEXTRAN SYSTEMS 5. 폴리머 용액의 제거법 6. Other Partitioning Systems 7. Reversed Micelles | |
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| 10. | |
Principles of chromatography | 1. Column Chromatography 2. Liquid Chromatography Columns 3. Liquid Chromatography 4. Fast Protein Liquid Chromatography (FPLC) 5. High Pressure Liquid Chromatography (HPLC) 6. Chromatographic Methods 7. The Number of Theoretical Plates 8. he Height Equivalent to a Theoretical Plate (HETP) 9. The Peak Asymmetry Factor 10. The Tailing Factor 11. Chromatographic Resolution 12. Resolution, R 13. Chromatographic Methods | |
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Chromatography techniques | 1. Sample Preparation 2. Purification Techniques 3. Principles of Chromatography 4. Factors Affecting Resolution of Chromatography 5. Effect of Temperature on Resolution 6. Effect of Flow Rate of Mobile Phase 7. Effect of Sample Volume and Concentration 8. Effect of Particles of Stationary Phase 9. Chromatography Types 10. Chromatography Techniques | |
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| 11. | |
Gel Filtration Chromatography | 1. Gel Filtration (Size Exclusion) Chromatography 2. Dextran Gels (Sephadex) 3. Sephadex Media 4. Sephadex Fraction Ranges (GE Healthcare) 5. Agarose Gels (Sepharose) 6. Sepharose Media 7. Sepharose Fraction Ranges (GE Healthcare) 8. Polyacrylamide Gels (Sephacryl) 9. Sephacryl Fraction Ranges (GE Healthcare) 10. Commercial Gel Matrix Media 11. Other Gel Matrix Media | |
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Gel Filtration Techniques | 1. Gel Filtration Chromatography 2. Advantages of Gel Chromatography 3. 시료의 준비 4. Gel Matrix Beads의 전처리 5. Sephadex Gel Type 6. Swelling of Gel Matrix Beads 7. Void (Vo) and Elution (Ve) Volume 8. Gel Filtration Chromatography 9. Parameters for Optimal Resolution in Gel Filtration Chromatography 10. Gel Beads의 재생과 보존 11. Considerations for Scale-up of Gel Chromatography | |
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| 12. | |
Ion Exchange Chromatography | 1. Ion Exchange Chromatography 2. Cation Exchanger 3. Anion Exchanger 4. Ion Exchange Chromatography 5. Elution with NaCl buffer 6. Ion Exchange Charge Groups 7. Comparison of Typical Ion Exchange Media 8. Ion Exchanger Based on the Sepharose Matrix 9. Ion Exchanger Based on the Sephadex Matrix 10. Meaning of Strong and Weak Exchangers 11. Effect of Buffer pH on the Weak and Strong Exchangers | |
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Ion Exchange Techniques | 1. Protein Net Charge 2. Buffers for Cation and Anion Exchangers 3. Typical Buffers for Cation and Anion Exchange Chromatography 4. Test for Starting pH 5. Advantages of Ion Exchange Chromatography 6. Gradient Maker 7. Linear Gradient Elution 8. Stepwise Gradient Elution 9. 이온교환체의 재사용과 보존 10. Considerations for Scale-up of Ion Exchange Chromatography | |
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| 13. | |
Hydrophobic Interaction Chromatography | 1. Ligand of Hydrophobic Interaction Chromatography 2. Hydrophobic Interaction Chromatography 3. Linear Gradient Elution of HIC 4. Factors Affecting HIC 5. HIC Sepharose Media 6. Salt Effect on HIC 7. pH Effect on HIC 8. Temperature Effect on HIC 9. Advantages of HIC | |
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Affinity Chromatography | 1. Affinity Chromatography의 원리 2. Matrices for Affinity Chromatography 3. General Ligands and Proteins for Affinity Chromatography 4. Affinity-tagged Fusion Proteins 5. His-tagged Fusion Protein 6. Elution of His tagged proteins 7. Glutathione S-transferase (GST) Fusion Protein 8. (GST+HIS)-Double tagged Fusion Protein 9. Maltose Binding Protein (MBP) Fusion Protein 10. Metal-Chelating Sepharose 11. Strep(SAWRHPQFGG)-tagged Fusion Protein 12. FLAG (DYKDDDDK)-tagged Fusion Protein 13. Binding Protein A/G to Fc Region 14. Various Affinity Chromatography (GE Healthcare) 15. Various Affinity Sepharose Media (GE Healthcare) | |
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| 14. | |
Other Chromatographies (RPC, IFC) | 1. Reversed Phase Chromatography 2. Polar and Nonpolar Molecules 3. Mechanism of Reversed Phase Chromatography 4. Comparison of RPC and HIC 5. Isoelectric Focusing (IEF) 6. Isofocusing Chromatography 7. Mechanism of Isofocusing Chromatography 8. Beads for Chromatofocusing | |
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Overall Review of Bioseparation Processes | 1. Monitoring Purification Steps 2. (A) Purification Process of Recombinant Somatotropin 3. (A) Yields and Purities of Steps in Purification of Somatotropin, Starting with 260kg of Inclusion Bodies 4. (B) Purification Process of Recombinant Human Leukocyte Interferon 5. (B) Yields and Purities of Steps in Purification of alpha-Interferon 6. (C) Purification Process of Recombinant L-Leucine Dehydrogenase 7. (C) Yields and Purities of Steps in Purification of L-leucine dehydrogenase 8. (D) Purification Process of Recombinant Tissue Plasminogen Activator | |
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