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

Tomonori Mishima, Takatoshi Ohkuri, Taiji Imoto, Tadashi Ueda

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2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2072-2074
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume71
Issue number8
DOIs
Publication statusPublished - Nov 21 2007

Fingerprint

disulfide bonds
Muramidase
lysozyme
Disulfides
Cysteine
cysteine
Enzymes
Modulation
Egg White
mutants
egg albumen
hens
hen egg lysozyme

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biotechnology
  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology
  • Food Science

Cite this

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AU - Mishima, Tomonori

AU - Ohkuri, Takatoshi

AU - Imoto, Taiji

AU - Ueda, Tadashi

PY - 2007/11/21

Y1 - 2007/11/21

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