Proline Isomerization in Unfolded Ribonuclease A
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1982.tb06935.x/fullpdf
Reference26 articles.
1. Both the Fast and Slow Refolding Reactions of Ribonuclease A Yield Native Enzyme
2. Guanidine-unfolded state of ribonuclease A contains both fast- and slow-refolding species.
3. Nature of the fast and slow refolding reactions of iron(III) cytochrome c
4. Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme
5. Further evidence suggesting that the slow phase in protein unfolding and refolding is due to proline isomerization: a kinetic study of carp parvalbumins
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