Skip Navigation



Journal of Biochemistry Advance Access published online on July 4, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn088
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
144/4/457    most recent
mvn088v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Fukunaga, Y.
Right arrow Articles by Yamashita, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fukunaga, Y.
Right arrow Articles by Yamashita, S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Japanese Biochemical Society

The Unfolding of {alpha}-Momorcharin Proceeds through the Compact Folded Intermediate

Yukihiro Fukunaga, Etsuko Nishimoto, Takuhiro Otosu, Yasutaka Murakami and Shoji Yamashita*

Institute of Biophysics, Faculty of Agriculture, Kyushu University, Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan

*To whom correspondence should be addressed: Shoji Yamashita. Tel/Fax: +81-92-642-4425, E-mail: yamashita{at}brs.kyushu-u.ac.jp

Received April 9, 2008; Accepted July 1, 2008


  Abstract

The unfolding of {alpha}-momorcharin was systematically investigated using steady-state and time-resolved tryptophan fluorescence, circular dichroism, and 8-anilino-1-naphthalenesulfonic acid (ANS) binding. These spectroscopic studies demonstrated that {alpha}-momorcharin unfolded through a compact folded intermediate state. The content of {alpha}-helix was increased, Trp192 approached closer to the side of active site and its rotational motion was restricted by being equilibrated with 2-3M of guanidine hydrochloride. Furthermore, the binding of ANS with {alpha}-momorcharin was more suppressed to show that the hydrophobic parts would not be accessed to the protein surface but rather be sealed off in this specific conformation state. These results suggest that the structure of {alpha}-momorcharin holds the more compact conformation as an incipient state for unfolding, which is the sharp contrast to β-momorcharin which gives the characteristics of the generally known molten globule state.

Key Words: {alpha}-momorcharin, protein folding/unfolding, molten globule, fluorescence energy transfer, time-resolved fluorescence depolarization


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.