Molecular chaperones / edited by George H. Lorimer, Thomas O. Baldwin.
The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. More th...
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Full Text (via ScienceDirect) |
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| Other Authors: | , |
| Format: | eBook |
| Language: | English |
| Published: |
San Diego :
Academic Press,
©1998.
|
| Series: | Methods in enzymology ;
v. 290. |
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Table of Contents:
- 1. Protein folding and assembly in a cell-free expression system
- 2. Preparation and application of chaperone-deficient Escherichia coli cell-free translation systems
- 3. Protein disulfide isomerase
- 4. Thermophilic fungal protein disulfide isomerase
- 5. Disulfide bond catalysts in Escherichia coli
- 6. Yeast immunophilins: Purification and assay of yeast FKBP12
- 7. Peptidylprolyl cis-trans-isomerases from plant organelles
- 8. Purification of GroEL with low fluorescence background
- 9. Overexpression, purification, and properties of GroES from Escherichia coli
- 10. Criteria for assessing the purity and quality of GroEL.
- 11. Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL
- 12. Chaperonin 60₁4 and co-chaperonin 10--from Chromatium vinosum
- 13. Chaperonins of the purple nonsulfur bacterium Rhodobacter sphaeroides
- 14. Chaperonins from Thermoanaerobacter species
- 15. Chaperonin from thermophile Thermus thermophilus
- 16. Insect chaperonin 60: Symbionin
- 17. Purification of yeast mitochondrial chaperonin 60 and co-chaperonin 10
- 18. Purification of Mammalian mitochondrial chaperonin 60 through in Vitro reconstitution of active oligomers
- 19. Purification of recombinant plant and animal GroES homologs: Chloroplast and mitochondrial chaperonin 10.