Heterogeneous packing in the folding/unfolding intermediate state of bitter gourd trypsin inhibitor

Daisuke Takahashi, Shuzo Matsumoto, Etsuko Nishimoto, Takuhiro Otosu, Shoji Yamashita

研究成果: ジャーナルへの寄稿記事

1 引用 (Scopus)

抄録

The conformation and dynamics of a protein are essential in characterizing the protein folding/unfolding intermediate state. They are closely involved in the packing and site-specific interactions of peptide elements to build and stabilize the tertiary structure of the protein. In this study, it was confirmed that trypsin inhibitor obtained from seeds of bitter gourd (BGTI) adopted a peculiar but plausible conformation and dynamics in the unfolding intermediate state. The fluorescence spectrum of one of two tryptophan residues of BGTI, Trp9, shifted to the blue side in the presence of 2-3M guanidine hydrochloride, although the other, Trp54, did not show this spectral shift. At the same time, the motional freedom of Trp9 revealed by a timeresolved fluorescence study decreased, suggesting that the segmental motion of this residue was more restricted. These results indicate that BGTI takes such a conformation state that the hydrophobic core and loop domains arranging Trp9 and Trp54 respectively are heterogeneously packed in the unfolding intermediate state.

元の言語英語
ページ(範囲)1498-1505
ページ数8
ジャーナルBioscience, Biotechnology and Biochemistry
72
発行部数6
DOI
出版物ステータス出版済み - 7 1 2008

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Momordica charantia
Trypsin Inhibitors
Conformations
Fluorescence
Protein Unfolding
Protein Folding
Guanidine
Tertiary Protein Structure
Tryptophan
Protein folding
Seeds
Peptides
Seed
Proteins

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

これを引用

Heterogeneous packing in the folding/unfolding intermediate state of bitter gourd trypsin inhibitor. / Takahashi, Daisuke; Matsumoto, Shuzo; Nishimoto, Etsuko; Otosu, Takuhiro; Yamashita, Shoji.

:: Bioscience, Biotechnology and Biochemistry, 巻 72, 番号 6, 01.07.2008, p. 1498-1505.

研究成果: ジャーナルへの寄稿記事

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AU - Matsumoto, Shuzo

AU - Nishimoto, Etsuko

AU - Otosu, Takuhiro

AU - Yamashita, Shoji

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N2 - The conformation and dynamics of a protein are essential in characterizing the protein folding/unfolding intermediate state. They are closely involved in the packing and site-specific interactions of peptide elements to build and stabilize the tertiary structure of the protein. In this study, it was confirmed that trypsin inhibitor obtained from seeds of bitter gourd (BGTI) adopted a peculiar but plausible conformation and dynamics in the unfolding intermediate state. The fluorescence spectrum of one of two tryptophan residues of BGTI, Trp9, shifted to the blue side in the presence of 2-3M guanidine hydrochloride, although the other, Trp54, did not show this spectral shift. At the same time, the motional freedom of Trp9 revealed by a timeresolved fluorescence study decreased, suggesting that the segmental motion of this residue was more restricted. These results indicate that BGTI takes such a conformation state that the hydrophobic core and loop domains arranging Trp9 and Trp54 respectively are heterogeneously packed in the unfolding intermediate state.

AB - The conformation and dynamics of a protein are essential in characterizing the protein folding/unfolding intermediate state. They are closely involved in the packing and site-specific interactions of peptide elements to build and stabilize the tertiary structure of the protein. In this study, it was confirmed that trypsin inhibitor obtained from seeds of bitter gourd (BGTI) adopted a peculiar but plausible conformation and dynamics in the unfolding intermediate state. The fluorescence spectrum of one of two tryptophan residues of BGTI, Trp9, shifted to the blue side in the presence of 2-3M guanidine hydrochloride, although the other, Trp54, did not show this spectral shift. At the same time, the motional freedom of Trp9 revealed by a timeresolved fluorescence study decreased, suggesting that the segmental motion of this residue was more restricted. These results indicate that BGTI takes such a conformation state that the hydrophobic core and loop domains arranging Trp9 and Trp54 respectively are heterogeneously packed in the unfolding intermediate state.

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