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        [资源] 申请上传 Current Protocols In Protein Science (60M) 见公共邮箱

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        如题。

        本书全面介绍目前蛋白质技术理论及应用,全书共 3843 页,够厚的吧。目录如下。

        Chapter 1 Strategies of Protein Purification and Characterization
        Unit 1.1 Overview of Protein Purification and Characterization
        Unit 1.2 Strategies for Protein Purification
        Unit 1.3 Protein Purification Flow Charts
        Unit 1.4 Purification of Glutamate Dehydrogenase from Liver and Brain
        Unit 1.5 Overview of the Physical State of Proteins within Cells
        Chapter 2 Computational Analysis
        Introduction
        Unit 2.1 Computational Methods for Protein Sequence Analysis
        Unit 2.2 Hydrophobicity Profiles for Protein Sequence Analysis
        Unit 2.3 Protein Secondary Structure Prediction
        Unit 2.4 Internet Basics
        Unit 2.5 Sequence Similarity Searching Using the BLAST Family of Programs
        Unit 2.6 Protein Databases on the Internet
        Unit 2.7 Protein Tertiary Structure Prediction
        Unit 2.8 Protein Tertiary Structure Modeling
        Unit 2.9 Comparative Protein Structure Prediction
        Chapter 3 Detection and Assay Methods
        Introduction
        Unit 3.1 Spectrophotometric Determination of Protein Concentration
        Unit 3.2 Quantitative Amino Acid Analysis
        Unit 3.3 In Vitro Radiolabeling of Peptides and Proteins
        Unit 3.4 Assays for Total Protein
        Unit 3.5 Kinetic Assay Methods
        Unit 3.6 Biotinylation of Proteins in Solution and on Cell Surfaces
        Unit 3.7 Metabolic Labeling with Amino Acids
        Unit 3.8 Analysis of Selenocysteine-Containing Proteins
        Unit 3.9 Solid-Phase Profiling of Proteins
        Chapter 4 Extraction, Stabilization, and Concentration
        Introduction
        Unit 4.1 Overview of Cell Fractionation
        Unit 4.2 Purification of Organelles from Mammalian Cells
        Unit 4.3 Subcellular Fractionation of Tissue Culture Cells
        Unit 4.4 Desalting, Concentration, and Buffer Exchange by Dialysis and Ultrafiltration
        Unit 4.5 Selective Precipitation of Proteins
        Unit 4.6 Long-Term Storage of Proteins
        Chapter 5 Production of Recombinant Proteins
        Introduction
        Unit 5.1 Production of Recombinant Proteins in Escherichia coli
        Unit 5.2 Selection of Escherichia coli Expression Systems
        Unit 5.3 Fermentation and Growth of Escherichia coli for Optimal Protein Production
        Unit 5.4 Overview of the Baculovirus Expression System
        Unit 5.5 Protein Expression in the Baculovirus System
        Unit 5.6 Overview of Protein Expression in Saccharomyces cerevisiae
        Unit 5.7 Overview of Protein Expression in Pichia pastoris
        Unit 5.8 Culture of Yeast for the Production of Heterologous Proteins
        Unit 5.9 Overview of Protein Expression by Mammalian Cells
        Unit 5.10 Production of Recombinant Proteins in Mammalian Cells
        Unit 5.11 Overview of the Vaccinia Virus Expression System
        Unit 5.12 Preparation of Cell Cultures and Vaccinia Virus Stocks
        Unit 5.13 Generation of Recombinant Vaccinia Viruses
        Unit 5.14 Characterization of Recombinant Vaccinia Viruses and Their Products
        Unit 5.15 Gene Expression Using the Vaccinia Virus/ T7 RNA Polymerase Hybrid System
        Unit 5.16 Choice of Cellular Protein Expression System
        Unit 5.17 Use of the Gateway System for Protein Expression in Multiple Hosts
        Chapter 6 Purification of Recombinant Proteins
        Introduction
        Unit 6.1 Overview of the Purification of Recombinant Proteins Produced in Escherichia coli
        Unit 6.2 Preparation of Soluble Proteins from Escherichia coli
        Unit 6.3 Preparation and Extraction of Insoluble (Inclusion-Body) Proteins from Escherichia coli
        Unit 6.4 Overview of Protein Folding
        Unit 6.5 Folding and Purification of Insoluble (Inclusion Body) Proteins from Escherichia coli
        Unit 6.6 Expression and Purification of GST Fusion Proteins
        Unit 6.7 Expression and Purification of Thioredoxin Fusion Proteins
        Chapter 7 Characterization of Recombinant Proteins
        Introduction
        Unit 7.1 Overview of the Characterization of Recombinant Proteins
        Unit 7.2 Determining the Identity and Purity of Recombinant Proteins by UV Absorption
        Spectroscopy
        Unit 7.3 Determining the Identity and Structure of Recombinant Proteins
        Unit 7.4 Transverse Urea-Gradient Gel Electrophoresis
        Unit 7.5 Analytical Ultracentrifugation
        Unit 7.6 Determining the CD Spectrum of a Protein
        Unit 7.7 Determining the Fluorescence Spectrum of a Protein
        Unit 7.8 Light Scattering
        Unit 7.9 Measuring Protein Thermostability by Differential Scanning Calorimetry
        Unit 7.10 Characterizing Recombinant Proteins Using HPLC Gel Filtration and Mass Spectrometry
        Unit 7.11 Rapid Screening of E. coli Extracts by Heteronuclear NMR
        Chapter 8 Conventional Chromatographic Separations
        Introduction
        Unit 8.1 Overview of Conventional Chromatography
        Unit 8.2 Ion-Exchange Chromatography
        Unit 8.3 Gel-Filtration Chromatography
        Unit 8.4 Hydrophobic-Interaction Chromatography
        Unit 8.5 Chromatofocusing
        Unit 8.6 Hydroxylapatite Chromatography
        Unit 8.7 HPLC of Peptides and Proteins
        Chapter 9 Affinity Purification
        Introduction
        Unit 9.1 Lectin Affinity Chromatography
        Unit 9.2 Dye Affinity Chromatography
        Unit 9.3 Affinity Purification of Natural Ligands
        Unit 9.4 Metal-Chelate Affinity Chromatography
        Unit 9.5 Immunoaffinity Chromatography
        Unit 9.6 Purification of Sequence-Specific DNA-Binding Proteins by Affinity Chromatography
        Unit 9.7 Purification of DNA-Binding Proteins Using Biotin/Streptavidin Affinity Systems
        Unit 9.8 Immunoprecipitation
        Unit 9.9 Overview of Affinity Tags for Protein Purification
        Chapter 10 Electrophoresis
        Introduction
        Unit 10.1 One-Dimensional SDS Gel Electrophoresis of Proteins
        Unit 10.2 One-Dimensional Isoelectric Focusing of Proteins in Slab Gels
        Unit 10.3 One-Dimensional Electrophoresis Using Nondenaturing Conditions
        Unit 10.4 Two-Dimensional Gel Electrophoresis
        Unit 10.5 Protein Detection in Gels Using Fixation
        Unit 10.6 Protein Detection in Gels Without Fixation
        Unit 10.7 Electroblotting from Polyacrylamide Gels
        Unit 10.8 Detection of Proteins on Blot Membranes
        Unit 10.9 Capillary Electrophoresis of Proteins and Peptides
        Unit 10.10 Immunoblot Detection
        Unit 10.11 Autoradiography
        Unit 10.12 Digital Electrophoresis Analysis
        Unit 10.13 Capillary Electrophoresis of Peptides and Proteins Using Isoelectric Buffers
        Chapter 11 Chemical Analysis
        Introduction
        Unit 11.1 Enzymatic Digestion of Proteins in Solution
        Unit 11.2 Enzymatic Digestion of Proteins on PVDF Membranes
        Unit 11.3 Digestion of Proteins in Gels for Sequence Analysis
        Unit 11.4 Chemical Cleavage of Proteins in Solution
        Unit 11.5 Chemical Cleavage of Proteins on Membranes
        Unit 11.6 Reversed-Phase Isolation of Peptides
        Unit 11.7 Removal of N-Terminal Blocking Groups from Proteins
        Unit 11.8 C-Terminal Sequence Analysis
        Unit 11.9 Amino Acid Analysis
        Unit 11.10 N-Terminal Sequence Analysis of Proteins and Peptides
        Unit 11.11 Determination of Disulfide-Bond Linkages in Proteins
        Chapter 12 Post-Translational Modification: Glycosylation
        Introduction
        Unit 12.1 Overview of Glycoconjugate Analysis
        Unit 12.2 Metabolic Radiolabeling of Animal Cell Glycoconjugates
        Unit 12.3 Inhibition of N-Linked Glycosylation
        Unit 12.4 Endoglycosidase and Glycoamidase Release of N-Linked Oligosaccharides
        Unit 12.5 Detection of Glycophospholipid Anchors on Proteins
        Unit 12.6 Determining the Structure of Oligosaccharides N- and O-Linked to Glycoproteins
        Unit 12.7 Determining the Structure of Glycan Moieties by Mass Spectrometry
        Unit 12.8 Detection and Analysis of Proteins Modified by O-Linked N-Acetylglucosamine
        Chapter 13 Post-Translational Modification: Phosphorylation and
        Phosphatases
        Introduction
        Unit 13.1 Overview of Protein Phosphorylation
        Unit 13.2 Labeling Cultured Cells with 32Pi and Preparing Cell Lysates for Immunoprecipitation
        Unit 13.3 Phosphoamino Acid Analysis
        Unit 13.4 Detection of Phosphorylation by Immunological Techniques
        Unit 13.5 Detection of Phosphorylation by Enzymatic Techniques
        Unit 13.6 Preparation and Application of Polyclonal and Monoclonal Sequence-Specific Anti-
        Phosphoamino Acid Antibodies
        Unit 13.7 Assays of Protein Kinases Using Exogenous Substrates
        Unit 13.8 Permeabilization Strategies to Study Protein Phosphorylation
        Unit 13.9 Phosphopeptide Mapping and Identification of Phosphorylation Sites
        Unit 13.10 Use of Protein Phosphatase Inhibitors
        Chapter 14 Post-Translational Modification: Specialized Applications
        Introduction
        Unit 14.1 Analysis of Disulfide Bond Formation
        Unit 14.2 Analysis of Protein Acylation
        Unit 14.3 Analysis of Protein Prenylation and Carboxyl-Methylation
        Unit 14.4 Analysis of Oxidative Modification of Proteins
        Unit 14.5 Analysis of Protein Ubiquitination
        Unit 14.6 Analysis of Protein S-Nitrosylation
        Chapter 15 Chemical Modification of Proteins
        Introduction
        Unit 15.1 Modification of Cysteine
        Unit 15.2 Modification of Amino Groups
        Chapter 16 Mass Spectrometry
        Introduction
        Unit 16.1 Overview of Peptide and Protein Analysis by Mass Spectrometry
        Unit 16.2 Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Analysis of Peptides
        Unit 16.3 Sample Preparation for MALDI Mass Analysis of Peptides and Proteins
        Unit 16.4 In-Gel Digestion of Proteins for MALDI-MS Fingerprint Mapping
        Unit 16.5 Searching Sequence Databases Over the Internet: Protein Identification Using MS-Fit
        Unit 16.6 Searching Sequence Databases Over the Internet: Protein Identification Using MS-Tag
        Unit 16.7 Enzymatic Approaches for Obtaining Amino Acid Sequence: On-Target Ladder
        Sequencing
        Unit 16.8 Introducing Samples Directly into Electrospray Ionization Mass Spectrometers Using a
        Nanospray Interface
        Unit 16.9 Introducing Samples Directly into Electrospray Ionization Mass Spectrometers Using
        Microscale Capillary Liquid Chromatography
        Unit 16.10 Protein Identification Using a Quadrupole Ion Trap Mass Spectrometer and SEQUEST
        Database Matching
        Unit 16.11 De Novo Peptide Sequencing via Manual Interpretation of MS/MS Spectra
        Chapter 17 Structural Biology
        Introduction
        Unit 17.1 Overview of Protein Structural and Functional Folds
        Unit 17.2 Overview of Macromolecular Electron Microscopy: An Essential Tool in Protein
        Structural Analysis
        Unit 17.3 Principles of Macromolecular X-Ray Crystallography
        Unit 17.4 Crystallization of Macromolecules
        Unit 17.5 Introduction to NMR of Proteins
        Unit 17.6 Probing Protein Structure and Dynamics by Hydrogen Exchange—Mass Spectrometry
        Unit 17.7 Introduction to Atomic Force Microscopy (AFM) in Biology
        Unit 17.8 Raman Spectroscopy of Proteins
        Chapter 18 Preparation and Handling of Peptides
        Introduction
        Unit 18.1 Introduction to Peptide Synthesis
        Unit 18.2 Synthesis of Multiple Peptides on Plastic Pins
        Unit 18.3 Synthetic Peptides for Production of Antibodies that Recognize Intact Proteins
        Unit 18.4 Native Chemical Ligation of Polypeptides
        Unit 18.5 Synthesis and Application of Peptide Dendrimers As Protein Mimetics
        Unit 18.6 Disulfide Bond Formation in Peptides
        Chapter 19 Identification of Protein Interactions
        Introduction
        Unit 19.1 Analysis of Protein-Protein Interactions
        Unit 19.2 Interaction Trap/Two-Hybrid System to Identify Interacting Proteins
        Unit 19.3 Phage-Based Expression Cloning to Identify Interacting Proteins
        Unit 19.4 Detection of Protein-Protein Interactions by Coprecipitation
        Unit 19.5 Imaging Protein-Protein Interactions by Fluorescence Resonance Energy Transfer (FRET)
        Microscopy
        Unit 19.6 High-Throughput Screening for Protein-Protein Interactions Using Yeast Two-Hybrid
        Arrays
        Unit 19.7 Identification of Protein Interactions by Far Western Analysis
        Unit 19.8 Scintillation Proximity Assay (SPA) Technology to Study Biomolecular Interactions
        Chapter 20 Quantitation of Protein Interactions
        Introduction
        Unit 20.1 Overview of the Quantitation of Protein Interactions
        Unit 20.2 Measuring Protein Interactions by Optical Biosensors
        Unit 20.3 Analytical Centrifugation: Equilibrium Approach
        Unit 20.4 Titration Microcalorimetry
        Unit 20.5 Reduced-Scale Large-Zone Analytical Gel-Filtration Chromatography for Measurement
        of Protein Association Equilibria
        Unit 20.6 Size-Exclusion Chromatography with On-Line Light Scattering
        Unit 20.7 Analytical Ultracentrifugation: Sedimentation Velocity Analysis
        Chapter 21 Peptidases
        Introduction
        Unit 21.1 Proteases
        Unit 21.2 Papain-like Cysteine Proteases
        Unit 21.3 Overview of Pepsin-like Aspartic Peptidases
        Unit 21.4 Metalloproteases
        Unit 21.5 Purification and Characterization of Proteasomes from Saccharomyces cerevisiae
        Unit 21.6 Purification of the Eukaryotic 20S Proteasome
        Unit 21.7 Serpins (Serine Protease Inhibitors)
        Unit 21.8 Caspases
        Unit 21.9 Use of GFP as a Reporter for the Analysis of Sequence-Specific Proteases
        Unit 21.10 An Overview of Serine Proteases
        Unit 21.11 Over-Expression and Purification of Active Serine Proteases and Their Variants from
        Escherichia coli Inclusion Bodies
        Unit 21.12 Assaying Proteases in Cellular Environments
        Unit 21.13 Expression, Purification, and Characterization of Caspases
        Unit 21.14 Expression, Purification, and Characterization of Aspartic Endopeptidases: Plasmodium
        Plasmepsins and "Short" Recombinant Human Pseudocathepsin
        Unit 21.15 Zymography of Metalloproteinases
        Unit 21.16 Monitoring Metalloproteinase Activity Using Synthetic Fluorogenic Substrates
        Unit 21.17 Applications for Chemical Probes of Proteolytic Activity
        Chapter 22 Gel-Based Proteome Analysis
        Introduction
        Unit 22.1 Overview of Proteome Analysis
        Unit 22.2 Protein Profiling Using Two-Dimensional Difference Gel Electrophoresis (2-D DIGE)
        Unit 22.3 Laser Capture Microdissection for Proteome Analysis
        Unit 22.4 Preparing Protein Extracts for Quantitative Two-Dimensional Gel Comparison
        Unit 22.5 Isolation of Organelles and Prefractionation of Protein Extracts Using Free-Flow
        Electrophoresis
        Chapter 23 Non-Gel-Based Proteome Analysis
        Introduction
        Unit 23.1 Analysis of Protein Composition Using Multidimensional Chromatography and Mass
        Spectrometry
        Unit 23.2 Quantitative Protein Profile Comparisons Using the Isotope-Coded Affinity Tag Method
        Unit 23.3 Proteomic Analysis Using 2-D Liquid Separations of Intact Proteins From Whole-Cell
        Lysates
        Unit 23.4 Quantitative Protein Analysis Using Proteolytic [18O]Water Labeling
        Appendix 1 Useful Data
        1A Characteristics of Amino Acids
        1B Commonly Used Detergents
        1C Conversion Factors and Half-Life Information for Radioactivity
        1D Common Conversion Factors
        Appendix 2 Laboratory Guidelines, Equipment, and Stock Solutions
        2A Laboratory Safety
        2B Safe Use of Radioisotopes
        2C Centrifuges and Rotors
        2D Standard Laboratory Equipment
        2E Commonly Used Reagents
        Appendix 3 Commonly Used Techniques
        3A Use of Protein Folding Reagents
        3B Dialysis
        3C Techniques for Mammalian Cell Tissue Culture
        3D Importing Biological Materials
        3E Silanizing Glassware
        3F Protein Precipitation Using Ammonium Sulfate
        3G Statistics: Detecting Differences Among Groups
        3H Analyzing Radioligand Binding Data
        Appendix 4 Molecular Biology Techniques
        4A Media Preparation and Bacteriological Tools
        4B Growth in Liquid or Solid Media
        4C Preparation of Plasmid DNA
        4D Introduction of Plasmid DNA into Cells
        4E Purification and Concentration of DNA from Aqueous Solutions
        4F Agarose Gel Electrophoresis
        4G Southern Blotting
        4H Hybridization Analysis of DNA Blots
        4I Digestion of DNA with Restriction Endonucleases
        4J The Polymerase Chain Reaction
        4K Quantitation of Nucleic Acids with Absorption Spectroscopy
        4L Growth and Manipulation of Yeast
        Appendix 5 Biophysical Methods: Data Analysis
        5A Theoretical Aspects of the Quantitative Characterization of Ligand Binding
        SUPPLIERS APPENDIX
        Selected Suppliers of Reagents and Equipment
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