E. coli Gene Expression Protocols /
Autor Corporativo: | |
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Otros Autores: | |
Formato: | eBook |
Lenguaje: | English |
Publicado: |
Totowa, NJ :
Humana Press : Imprint: Humana,
2003.
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Edición: | 1st ed. 2003. |
Colección: | Methods in Molecular Biology,
205 |
Materias: |
Tabla de Contenidos:
- Cold-Inducible Promoters for Heterologous Protein Expression
- Dual-Expression Vectors for Efficient Protein Expression in Both E. coli and Mammalian Cells
- A Dual-Expression Vector Allowing Expression in E. coli and P. pastoris, Including New Modifications
- Purification of Recombinant Proteins from E. coli by Engineered Inteins
- Calmodulin as an Affinity Purification Tag
- Calmodulin-Binding Peptide as a Removable Affinity Tag for Protein Purification
- Maltose-Binding Protein as a Solubility Enhancer
- Thioredoxin and Related Proteins as Multifunctional Fusion Tags for Soluble Expression in E. coli
- Discovery of New Fusion Protein Systems Designed to Enhance Solubility in E. coli
- Assessment of Protein Folding/Solubility in Live Cells
- Improving Heterologous Protein Folding via Molecular Chaperone and Foldase Co-Expression
- High-Throughput Purification of PolyHis-Tagged Recombinant Fusion Proteins
- Co-Expression of Proteins in E. coli Using Dual Expression Vectors
- Small-Molecule Affinity-Based Matrices for Rapid Protein Purification
- Use of tRNA-Supplemented Host Strains for Expression of Heterologous Genes in E. coli
- Screening Peptide/Protein Libraries Fused to the ? Repressor DNA-Binding Domain in E. coli Cells
- Studying Protein-Protein Interactions Using a Bacterial Two-Hybrid System
- Using Bio-Panning of FLITRX Peptide Libraries Displayed on E. coli Cell Surface to Study Protein-Protein Interactions
- Use of Inteins for the In Vivo Production of Stable Cyclic Peptide Libraries in E. coli
- Hyperphage
- Combinatorial Biosynthesis of Novel Carotenoids in E. coli
- Using Transcriptional-Based Systems for In Vivo Enzyme Screening
- Identification of Genes Encoding Secreted Proteins Using Mini-OphoA Mutagenesis.