Insoluble Proteins
Springer-Verlag New York Inc.
978-1-0716-1861-5 (ISBN)
Authoritative and cutting-edge, Insoluble Proteins: Methods and Protocols, Second Edition aims to be a useful practical guide to researches to help further their study in this field.
General Introduction: Recombinant protein production and purification of insoluble proteins.- Overcoming the solubility problem in E. coli: available approaches for recombinant protein production.- A3D 2.0 update for the prediction and optimization of protein solubility.- Tailoring codon usage to the underlying biology for protein expression optimization.- Protein Expression Optimization Strategies in E. coli: A Tailored Approach in Strain Selection and Parallelizing Expression Conditions.- A novel approach for production of aggregation prone proteins using the spidroin-derived NT* tag.- Cleavable Self-Aggregating Tags (cSAT) for Therapeutic Peptide Expression and Purification.- Use Intein Cleavable Polyhydroxyalkanoate Synthase Fusions to Improve Protein Solubility.- Introduction of a hexalysine (6K) tag can protect from N-terminal cleavage and increase yield of recombinant proteins expressed in the periplasm of E. coli.- Two-tiered selection and screening strategy to increase functional enzyme production in Escherichia coli.- Method for production of cysteine-rich proteins in Lactococcus lactis expression system.- Heterologous protein production in Lactobacillus (plantarum) using pSIP vectors.- Soluble recombinant protein production in Pseudoaltermonas haloplanktis TAC125: the case study of the full-length human CDKL5 protein.- A protocol to enhance soluble protein expression in the cytoplasm of Bacillus subtilis.- Applications of cell-free synthesized membrane protein precipitates.- High cell-density expression system: yeast cells in a phalanx efficiently produce a certain range of “difficult-to-express” secretory recombinant proteins.- Insect Cells-Baculovirus system for the production of difficult to express proteins: from expression screening for soluble constructs to protein quality control.- Transient gene expression in human Expi293 cells.- Recombinant Expression of Complex Proteins in Human Cells Lines.- Optimizing chaperone removal strategy from over-expressed recombinant proteins: GNE, a case study.- Intrinsically disordered proteins (IDP): purification under denaturing conditions.- Solubilization and Refolding of Inclusion Body Proteins.- Non-denaturing solubilization of Inclusion Bodies from Lactic Acid Bacteria.- Purification of Inclusion Bodies Produced in Bacteria and Yeast.- Eukaryotic aggresomes: protocols and tips for their production, purification and handling.- Characterization of the conformational properties of soluble and insoluble proteins by Fourier transform infrared spectroscopy.- Characterizing Soluble Protein Aggregates using Native Mass Spectrometry Coupled with Temperature-control Electrospray Ionization and Size-exclusion Chromatography.- Quality control of proteins solubilized from inclusion bodies.- Methods for the Characterizationof Protein Aggregates.- Insoluble Protein Applications: The Use of Bacterial Inclusion Bodies as Biocatalysts.- Methods for Processing Protein Aggregates into Surfaces.
| Erscheinungsdatum | 01.02.2023 |
|---|---|
| Reihe/Serie | Methods in Molecular Biology ; 2406 |
| Zusatzinfo | 60 Illustrations, color; 38 Illustrations, black and white; XVI, 533 p. 98 illus., 60 illus. in color. |
| Verlagsort | New York, NY |
| Sprache | englisch |
| Maße | 178 x 254 mm |
| Themenwelt | Naturwissenschaften ► Biologie ► Biochemie |
| Naturwissenschaften ► Biologie ► Mikrobiologie / Immunologie | |
| Schlagworte | Escherichia coli • Insect Cells-Baculovirus • Lactococcus lactis • Protein Solubility • Pseudoaltermonas haloplanktis TAC125 |
| ISBN-10 | 1-0716-1861-X / 107161861X |
| ISBN-13 | 978-1-0716-1861-5 / 9781071618615 |
| Zustand | Neuware |
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