Equilibrium unfolding of kinetically stable serine protease milin: the presence of various active and inactive dimeric intermediates
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Biophysics
Link
http://link.springer.com/content/pdf/10.1007/s00249-010-0593-z.pdf
Reference52 articles.
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3. Clark AC, Sinclair JF, Baldwin TO (1993) Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits. J Biol Chem 268:10773–10779
4. Cunningham EL, Jaswal SS, Sohl JL, Agard DA (1999) Kinetic stability as a mechanism for protease longevity. Proc Natl Acad Sci U S A 96:11008–11014
5. Dams T, Jaenicke R (1999) Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima. Biochemistry 38:9169–9178
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