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
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- MISHIMA Tomonori
- Graduate School of Pharmaceutical Sciences, Kyushu University
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- OHKURI Takatoshi
- Graduate School of Pharmaceutical Sciences, Kyushu University
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- IMOTO Taiji
- Faculty of Biotechnology and Life Science, Sojo University
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- UEDA Tadashi
- Graduate School of Pharmaceutical Sciences, Kyushu University
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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.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 71 (8), 2072-2074, 2007
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390282681455795072
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- NII Article ID
- 10027518126
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 8888165
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed
