Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560030603/fullpdf
Reference20 articles.
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2. Interactions between cysteine residues as probes of protein conformation: The disulphide bond between Cys-14 and Cys-38 of the pancreatic trypsin inhibitor;Creighton;J Mol Biol,1975
3. Disulphide bonds and protein stability;Creighton;BioEssays,1988
4. Kinetic role of a meta-stable nativelike two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor;Creighton;J Mol Biol,1984
5. A study of factors influencing the reactivation of reduced egg white lysozyme;Epstein;J Biol Chem,1963
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