Skip Navigation


Journal of Biochemistry Advance Access originally published online on December 13, 2006
Journal of Biochemistry 2007 141(1):9-18; doi:10.1093/jb/mvm002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
141/1/9    most recent
mvm002v1
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?

© 2006 The Japanese Biochemical Society.

The Partially Unfolded State of ß-Momorcharin Characterized with Steady-state and Time-resolved Fluorescence Studies

Yukihiro Fukunaga1, Etsuko Nishimoto1, Katsumi Yamashita2, Takuhiro Otosu1 and Shoji Yamashita1,*

1Institute of Biophysics, Faculty of Agriculture, Graduate School of Kyushu University, Higashiku, Fukuoka 812-8581, Japan; and 2VALWAY Technology Center, NEC Soft, Ltd., Shinkiba, Koto-ku, Tokyo 136-8608, Japan

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

Received September 1, 2006; Accepted November 2, 2006


  Abstract

The specific conformation of partially unfolded state of ß-momorcharin was characterized through the steady-state and time-resolved fluorescence spectroscopic studies on a single Trp-190 which located adjacently to the active site. The content of secondary structure was retained, the binding of ANS was remarkably enhanced, and the correlation time of entire protein rotation was prolonged at the partially unfolded state formed by being equilibrated with the mild concentration of guanidine hydrochloride. The time-resolved fluorescence depolarization and excitation energy transfer analysis suggest that Trp-190 approached 2 Å closer to Tyr-70 and was hidden from the exposure to the protein surface, while the rotational correlation time and freedom of its segmental motion were shortened and enhanced, respectively. These results suggest that the transient folding/unfolding intermediate state of ß-momorcharin adopt the specific conformation at the vicinity of the active site, although it exhibits very similar properties with those of the generally known molten-globule state.

Key Words: energy transfer, folding/unfolding, ß-momorcharin, molten-globule state, segmental motion of protein, time-resolved fluorescence

Abbreviations: ANS, 1,8-anilinophthalene sulfonate; CD, circular dichroism; Gdn, guanidine hydrochloride; MG, molten-globule; RIPs, ribosome-inactivating proteins; TCSPC, time-correlated single photon counting


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


This article has been cited by other articles:


Home page
 J BiochemHome page
T. Otosu, E. Nishimoto, and S. Yamashita
Spectrally and Time-resolved Fluorescence Spectroscopic Study on Melittin Calmodulin Interaction
J. Biochem., November 1, 2007; 142(5): 655 - 661.
[Abstract] [Full Text] [PDF]


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.