The folding and evolution of multidomain proteins
β Scribed by Han, Jung-Hoon; Batey, Sarah; Nickson, Adrian A.; Teichmann, Sarah A.; Clarke, Jane
- Book ID
- 109958737
- Publisher
- Nature Publishing Group
- Year
- 2007
- Tongue
- English
- Weight
- 663 KB
- Volume
- 8
- Category
- Article
- ISSN
- 1471-0072
- DOI
- 10.1038/nrm2144
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The beta 2 subunit of Escherichia coli tryptophan synthase can be either unfolded in 6 M guanidine, or extensively denatured at acidic pH. These two denatured forms of beta 2 have different circular dichroism spectra and thus correspond to distinct physical states. Here we compare the folding pathwa
An important idea that emerges from the energy landscape theory of protein folding is that subtle global features of the protein landscape can profoundly affect the apparent mechanism of folding. The relationship between various characteristic temperatures in the phase diagrams and landmarks in the