Folding of lysozyme
Author:
Publisher
Birkhäuser Basel
Link
http://link.springer.com/content/pdf/10.1007/978-3-0348-9225-4_9.pdf
Reference59 articles.
1. Acharya, A.S. and Taniuchi, H. (1976) A study of renaturation of reduced hen egg white lysozyme. J. Biol. Chem. 251: 6934–6946.
2. Acharya, A.S. and Taniuchi, H. (1977) Formation of the four isomers of hen egg white lysozyme containing three native disulfide bonds and one open disulfide bond. Proc. Natl. Acad. Sci. USA 74: 2362–2366.
3. Acharya, A.S. and Taniuchi, H. (1978) Reduction and renaturation of hen egg lysozyme containing carboxymethylcysteine-6 and -127. Biochemistry 17: 3064–3070.
4. Acharya, A.S. and Taniuchi, H. (1982) Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation. Mol. Cell. Biochem. 44: 129–148.
5. Anfinsen, C.B. (1973) Principles that govern the folding of protein chains. Science 181: 223–230.
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Heterologous Expression of Hen Egg White Lysozyme and Resonance Assignment of Tryptophan Side Chains in its Non-native States;Journal of Biomolecular NMR;2005-10
2. Calorimetric evidence for a native-like conformation of hen egg-white lysozyme dissolved in glycerol;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2000-05
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