The aggregation of cytochrome C may be linked to its flexibility during refolding
Author:
Publisher
Springer Science and Business Media LLC
Subject
Agricultural and Biological Sciences (miscellaneous),Environmental Science (miscellaneous),Biotechnology
Link
http://link.springer.com/content/pdf/10.1007/s13205-015-0345-y.pdf
Reference23 articles.
1. Akiyama S, Takahashi S et al (2000) Stepwise formation of α-helices during cytochrome c folding. Nat Struct Mol Biol 7(6):514–520
2. Akiyama S, Takahashi S et al (2002) Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle X-ray scattering. Proc Natl Acad Sci 99(3):1329–1334
3. Arai M, Kuwajima K (1996) Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Fold Des 1(4):275–287
4. Basu A, Li X et al (2011) Refolding of proteins from inclusion bodies: rational design and recipes. Appl Microbiol Biotechnol 92(2):241–251
5. Belton D (2008) The physical characterisation of protective antigen protein. University of Manchester
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