For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
7
views
0
references
 Top references
cited by
1
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      7
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: not found

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

      Author(s):
      Publication date:
      Journal: Bioscience, biotechnology, and biochemistry
      Keywords: Animals, Chickens, Muramidase, chemistry, Protein Folding

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          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.

          Related collections

          Author and article information

          Journal
          PubMed ID:: 15973056
          DOI:: 10.1271/bbb.69.1206

          ScienceOpen disciplines: Chemistry
          Keywords: Animals,Chickens,Muramidase,chemistry,Protein Folding
          Data availability:
          ScienceOpen disciplines: Chemistry
          Keywords: Animals, Chickens, Muramidase, chemistry, Protein Folding

          Comments

          Comment on this article