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Journal of Biochemistry Advance Access published online on December 13, 2006
Journal of Biochemistry, doi:10.1093/jb/mvm002
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© 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.
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@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: ß-momorcharin, energy transfer, folding/unfolding, molten-globule state, segmental motion of protein, time-resolved fluorescence


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