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Protein Engineering Handbook Eine ´´Werkzeugkiste´´ für den Biotechniker! Systematisch und praxisorientiert bietet dieses außergewöhnlich umfangreiche, zweibändige Handbuch eine Fülle an technischen, methodischen und anwendungsspezifischen Informationen zum Gesamtgebiet des Protein Engineering. 16.07.2012, PDF.

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Protein Engineering Handbook, Eine ´´Werkzeugkiste´´ für den Biotechniker! Systematisch und praxisorientiert bietet dieses aussergewöhnlich umfangreiche, zweibändige Handbuch eine Fülle an technischen, methodischen und anwendungsspezifischen Informationen zum Gesamtgebiet des Protein Engineering. PDF, 16.07.2012.

Lieferung aus: Deutschland, Versandkostenfrei.
Protein Engineering Handbook: InhaltsangabePreface XVList of Contributors XVII1 Dirigent Effects in Biocatalysis 1 Bettina M. Nestl, Bernd A. Nebel, and Bernhard Hauer1.1 Introduction 11.2 Dirigent Proteins 31.3 Solvents and Unconventional Reaction Media 41.3.1 Ionic Liquids 71.3.2 Microemulsions and Reversed Micelles Systems 101.4 Structure and Folding 121.5 Structured and Unstructured Domains 141.6 Isozymes, Moonlighting Proteins, and Promiscuity: Supertalented Enzymes 191.7 Conclusions 22Acknowledgment 23References 232 Protein Engineering Guided by Natural Diversity 29 James T. Kratzer, Megan F. Cole, and Eric A. Gaucher2.1 Approaches 292.1.1 Ancestral Sequence Reconstruction (ASR) 302.1.2 Ancestral Mutation Method 312.1.3 Reconstructing Evolutionary Adaptive Paths (REAP) 322.2 Protocols 342.2.1 Practical Steps to Using ASR 342.2.2 Reconstructing Evolutionary Adaptive Paths: A Focused Application of ASR 362.3 Future Directions 382.3.1 Industrial Applications 402.3.2 Biomedical 412.3.3 Drug Discovery 412.3.4 Paleobiology 422.3.5 Synthetic Biology 432.3.6 Experimental Validation of ASR 432.4 Conclusions 44References 443 Protein Engineering Using Eukaryotic Expression Systems 47 Martina Geier and Anton Glieder3.1 Introduction 473.2 Eukaryotic Expression Systems 483.2.1 Yeast Expression Platforms 483.2.1.1 Saccharomyces cerevisiae 483.2.1.2 Pichia pastoris 513.2.1.3 Pichia angusta 543.2.1.4 Alternative Yeasts 553.2.2 Filamentous Fungi 563.2.3 Insect Cells 583.2.4 Mammalian Cell Cultures 593.2.5 Transgenic Animals and Plants 613.2.6 Cell-Free Expression Systems 613.3 Conclusions 63References 654 Protein Engineering in Microdroplets 73 Yolanda Schaerli, Balint Kintses, and Florian Hollfelder4.1 Introduction 734.2 Droplet Formats 754.2.1 &ldquo Bulk&rdquo Emulsions 754.2.1.1 Catalytic Selections Involving DNA Substrates 764.2.1.2 Using the Droplet Compartment to Form a Permanent Genotype-Phenotype Linkage for Selections of Binders 774.2.2 Double &ldquo Bulk&rdquo Emulsions 784.2.3 Microfl uidic Droplets 794.3 Perspectives 83Acknowledgments 84References 845 Folding and Dynamics of Engineered Proteins 89 Michelle E. McCully and Valerie Daggett5.1 Introduction 895.2 Proof-of-Principle Protein Designs 905.2.1 FSD-1, a Heterogeneous Native State and Complicated Folding Pathway 915.2.2 &alpha 3D, a Dynamic Core Leads to Fast Folding and Thermal Stability 945.2.3 Three-Helix Bundle Thermostabilized Proteins 965.2.4 Top7, a Novel Fold Topology 975.2.5 Other Rosetta Designs 1005.3 Proteins Designed for Function 1025.3.1 Ligands 103 the Only Stability: Oxidative and Other Chemical Stabilities 1296.2.2.1 Oxidative Stability 1296.2.2.2 Stabilization against Aldehydes and Solvents 1306.2.2.3 Alkaline Tolerance 1316.3 Measurement of a Protein&rsquo s Kinetic Stability 1326.3.1 Materials and General Hints 1326.3.2 Thermal Stability 1326.3.2.1 Thermal Profi le 1326.3.2.2 Thermal Inactivation 1336.3.3 Measurement of Oxidative Stability 1346.3.4 Stability Analysis and Accelerated Degradation Testing 1356.3.4.1 Set-Up 1366.3.4.2 Analysis of Results 1376.4 Developments in Protein Stabilization 137References 1397 Enzymes from Thermophilic Organisms 145 Tamotsu Kanai and Haruyuki Atomi7.1 Introduction 1457.2 Hyperthermophiles 1467.3 Enzymes from Thermophiles and Their Reactions 1467.4 Production of Proteins from (Hyper)Thermophiles 1487.5 Protein Engineering of Thermophilic Proteins 1547.6 Cell Engineering in Hyperthermophiles 1567.7 Future Perspectives 157References 1578 Enzyme Engineering by Cofactor Redesign 163 Malgorzata M. Kopacz, Frank. Hollmann, and Marco W. Fraaije8.1 Introduction 1638.2 Natural Cofactors: Types, Occurrence, and Chemistry 1648.3 Inorganic Cofactors 1658.4 Organic Cofactors 1688.5 Redox Cofactors 1698.5.1 Nicotinamide Cofactor Engineering 1708.5.2 Heme Cofactor Engineering 1738.5.2.1 Reconstitution of Myoglobin 1748.5.2.2 Artificial Metalloproteins Based on Serum Albumins 1758.5.3 Flavin Cofactor Engineering 1768.6 Concluding Remarks 180References 1819 Biocatalyst Identifi cation by Anaerobic High-Throughput Screening of Enzyme Libraries and Anaerobic Microorganisms 193 Helen S. Toogood and Nigel S. Scrutton9.1 Introduction 1939.2 Oxygen-Sensitive Biocatalysts 1949.2.1 Flavoproteins 1949.2.2 Iron-Sulfur-Containing Proteins 1959.2.3 Other Causes of Oxygen Sensitivity 1979.3 Biocatalytic Potential of Oxygen-Sensitive Enzymes and Microorganisms 1989.3.1 Old Yellow Enzymes (OYEs) 1989.3.2 Enoate Reductases 2009.3.3 Other Enzymes 2029.3.4 Whole-Cell Anaerobic Fermentations 2029.4 Anaerobic High-Throughput Screening 2039.4.1 Semi-Anaerobic Screening Protocols 2049.4.2 Anaerobic Robotic High-Throughput Screening 2059.4.2.1 Purifi ed Enzyme versus Whole-Cell Extracts 2079.4.2.2 Indirect Kinetic Screening versus Direct Product Determination 2089.4.3 Potential Extensions of Robotic Anaerobic High-Throughput Screening 2099.5 Conclusions and Outlook 210References 21010 Organometallic Chemistry in Protein Scaffolds 215 Yvonne M. Wilson, Marc D&uuml rrenberger, and Thomas R. Ward10.1 Introduction 21510.1.1 Concept 21510.1.2 Considerations for Designing an Artifi cial Metalloenzyme 21610.1.2.1 Organometallic Complex 21610.1.2.2 Biomolecular Scaffold 21810.1.2.3 Anchoring Strategy 219< Expansion of Substrate Scope 23610.3.4 Upscaling 23610.3.5 Potential Applications 23710.4 Summary 237Acknowledgments 237References 23811 Engineering Protease Specificity 243 Philip N. Bryan11.1 Introduction 24311.1.1 Overview 24311.1.2 Some Basic Points 24411.1.2.1 Mechanism for a Serine Protease 24411.1.2.2 Measuring Specifi city 24411.1.2.3 Binding Interactions 24511.1.3 Nature versus Researcher 24711.1.3.1 P1 Specifi city of Chymotrypsin-like Proteases 24711.1.3.2 The S1 Site of Subtilisin 24711.1.3.3 The S4 Site of Subtilisin 25011.1.3.4 Other Subsites in Subtilisin 25011.1.3.5 Kinetic Coupling and Specifi city 25111.2 Protocol and Practical Considerations 25111.2.1 Remove and Regenerate 25111.2.2 Engineering Highly Stable and Independently Folding Subtilisins 25211.2.3 Engineering of P4 Pocket to Increase Substrate Specifi city 25311.2.4 Destroying the Active Site in Order to Save It 25411.2.5 Identifying a Cognate Sequence for Anion-Triggered Proteases Using the Subtilisin Prodomain 25511.2.6 Tunable Chemistry and Specifi city 25711.2.7 Purification Proteases Based on Prodomain&ndash Subtilisin Interactions and Triggered Catalysis 25811.2.8 Design of a Mechanism-Based Selection System 25911.2.8.1 Step 1: Ternary Complex Formation 25911.2.8.2 Step 2: Acylation 26311.2.8.3 Steps 3 and 4: Deacylation and Product Release 26511.2.9 Evolving Protease Specifi city Regulated with Anion Cofactors by Phage Display 26611.2.9.1 Construction and Testing of Subtilisin Phage 26611.2.9.2 Random Mutagenesis and Transformation 26711.2.9.3 Select, Englisch, Ebook.

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