A universal strategy for obtaining maximal protein expression or refolding remains elusive; however, headway has been made toward understanding these processes in vivo. The observation of reversible protein aggregation, asymmetry in protein--chaperone complexes, redox effects on disulfide formation,
Encyclopedia of Life Sciences || Protein Folding and Chaperones
β Scribed by Sinnige, Tessa
- Book ID
- 118126158
- Publisher
- John Wiley & Sons, Ltd
- Year
- 2010
- Tongue
- English
- Weight
- 459 KB
- Category
- Article
- ISBN-13
- 9780470015902
No coin nor oath required. For personal study only.
β¦ Synopsis
Articles In The Fields Of Biochemistry And Physiology, Cell Biology, Developmental Biology, Ecology, Evolution, Genetics, Immunology, Molecular Biology, Neuroscience, Microbiology And Virology, Plant Science, Structural Biology, Science And Society. Includes Index.
π SIMILAR VOLUMES
Articles In The Fields Of Biochemistry And Physiology, Cell Biology, Developmental Biology, Ecology, Evolution, Genetics, Immunology, Molecular Biology, Neuroscience, Microbiology And Virology, Plant Science, Structural Biology, Science And Society. Includes Index.
Articles In The Fields Of Biochemistry And Physiology, Cell Biology, Developmental Biology, Ecology, Evolution, Genetics, Immunology, Molecular Biology, Neuroscience, Microbiology And Virology, Plant Science, Structural Biology, Science And Society. Includes Index.
## Abstract The discovery of βmolecular chaperonesβ has dramatically changed our concept of cellular protein folding. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformation in a reaction mediated by these versatile helper proteins. Und