Literature DB >> 15973056

Characterization of refolded hen lysozyme variant lacking two outside disulfide bonds.

Takatoshi Ohkuri1, Taiji Imoto, Tadashi Ueda.   

Abstract

We characterized a refolded hen lysozyme variant containing only two SS-bonds, C64-C80 and C76-C94 (4CAHEL). From CD spectra and its activity, it was found that the refolded 4CAHEL has a structural topology analogous to wild-type lysozyme (WTHEL). Moreover, the refolded 4CAHEL showed no thermal transition, indicating that it had a character like a molten globule.

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Year:  2005        PMID: 15973056     DOI: 10.1271/bbb.69.1206

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  1 in total

1.  Reinvestigation of the oxidative folding pathways of hen egg white lysozyme: switching of the major pathways by temperature control.

Authors:  Kenta Arai; Wataru Shibagaki; Reina Shinozaki; Michio Iwaoka
Journal:  Int J Mol Sci       Date:  2013-06-26       Impact factor: 5.923

  1 in total

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