The unfolding of α-momorcharin proceeds through the compact folded intermediate

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

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


The unfolding of α-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 α-momorcharin unfolded through a compact folded intermediate state. The content of α-helix was increased, Trp192 approached closer to the side of active site and its rotational motion was restricted by being equilibrated with 2-3 M of guanidine hydrochloride. Furthermore, the binding of ANS with α-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 α-momorcharin holds the more compact conformation as an incipient state for unfolding, which is the sharp contrast to β-momorcharin that gives the characteristics of the generally known molten globule state.

Original languageEnglish
Pages (from-to)457-466
Number of pages10
JournalJournal of biochemistry
Issue number4
Publication statusPublished - Oct 2008

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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