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
-
- MISHIMA Tomonori
- Graduate School of Pharmaceutical Sciences, Kyushu University
-
- OHKURI Takatoshi
- Graduate School of Pharmaceutical Sciences, Kyushu University
-
- IMOTO Taiji
- Faculty of Biotechnology and Life Science, Sojo University
-
- UEDA Tadashi
- Graduate School of Pharmaceutical Sciences, Kyushu University
この論文をさがす
抄録
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.
収録刊行物
-
- Bioscience, Biotechnology, and Biochemistry
-
Bioscience, Biotechnology, and Biochemistry 71 (8), 2072-2074, 2007
公益社団法人 日本農芸化学会
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1390282681455795072
-
- NII論文ID
- 10027518126
-
- NII書誌ID
- AA10824164
-
- ISSN
- 13476947
- 09168451
-
- NDL書誌ID
- 8888165
-
- 本文言語コード
- en
-
- データソース種別
-
- JaLC
- NDL
- Crossref
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可