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Analyses of Native Disulfide Bond Formations in the Early Stage of the Folding Process in Mutant Lysozymes Where the Long-Range Interactions in the Denatured State Were Modulated
- Source :
- Bioscience, Biotechnology, and Biochemistry. 71:2072-2074
- Publication Year :
- 2007
- Publisher :
- Oxford University Press (OUP), 2007.
-
Abstract
- In order to clarify whether modulation of long-range interactions in the denatured state affect native disulfide bond (SS bond) formations of hen egg white lysozyme (HEL) containing a pair of cysteine residues, we examined the extent of SS bond formation among 12 variants containing a pair of cysteines. The loss of clusters 5 and 6 in the denatured state affected the formation of Cys30-Cys115 and Cys6-Cys127 respectively.
- Subjects :
- Protein Denaturation
Protein Folding
Stereochemistry
Mutant
Egg protein
Applied Microbiology and Biotechnology
Biochemistry
Analytical Chemistry
chemistry.chemical_compound
Animals
Disulfides
Molecular Biology
Muramidase
chemistry.chemical_classification
Egg Proteins
Organic Chemistry
General Medicine
Folding (chemistry)
Enzyme
chemistry
Mutation
Protein folding
Lysozyme
Chickens
Biotechnology
Cysteine
Subjects
Details
- ISSN :
- 13476947 and 09168451
- Volume :
- 71
- Database :
- OpenAIRE
- Journal :
- Bioscience, Biotechnology, and Biochemistry
- Accession number :
- edsair.doi.dedup.....4074aa689bf7db1712b7093d128dde5c
- Full Text :
- https://doi.org/10.1271/bbb.70155