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Titolo:
High pressure NMR study of a small protein, gurmarin
Autore:
Inoue, K; Yamada, H; Imoto, T; Akasaka, K;
Indirizzi:
Kobe1,niv, Grad Sch Sci & Technol, Div Mol Sci, Nada Ku, Kobe, Hyogo 657850 Kobe Univ Kobe Hyogo Japan 6578501 v Mol Sci, Nada Ku, Kobe, Hyogo 657850 Kobe Univ, Fac Sci, Dept Chem, Nada Ku, Kobe, Hyogo 6578501, Japan Kobe Univ Kobe Hyogo Japan 6578501 m, Nada Ku, Kobe, Hyogo 6578501, Japan Tottori Univ, Fac Med, Yonago, Tottori 6830826, Japan Tottori Univ YonagoTottori Japan 6830826 Yonago, Tottori 6830826, Japan
Titolo Testata:
JOURNAL OF BIOMOLECULAR NMR
fascicolo: 4, volume: 12, anno: 1998,
pagine: 535 - 541
SICI:
0925-2738(199811)12:4<535:HPNSOA>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-DYNAMICS SIMULATION; PROTON CHEMICAL-SHIFTS; SECONDARY STRUCTURE; RIBONUCLEASE-A; SPECTROSCOPY; EXCHANGE; WATER; COMPRESSIBILITY; CONFORMATION; VOLUME;
Keywords:
beta-sheet; compressibility; gurmarin; Gymnema sylvestre; high pressure NMR; hydrogen bond; tertiary structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Akasaka, K KobeKobe,, Grad Sch Sci & Technol, Div Mol Sci, Nada Ku, 1-1 Rokkodai-cho, Kobe Univ 1-1 Rokkodai-cho Kobe Hyogo Japan 6578501 kkodai-cho,
Citazione:
K. Inoue et al., "High pressure NMR study of a small protein, gurmarin", J BIOM NMR, 12(4), 1998, pp. 535-541

Abstract

The effect of pressure on the structure of gurmarin, a globular, 35-residue protein from Gymnema sylvestre, was studied in aqueous environment (95% (H2O)-H-1/5% (H2O)-H-2, pH 2.0) with an on-line variable pressure NMR systemoperating at 750 MHz. Two-dimensional TOCSY and NOESY spectra were measured as functions of pressure between 1 and 2000 bar at 40 degrees C. Practically all the proton signals of gurmarin underwent some shifts with pressure,showing that the entire protein structure responds to, and is altered by, pressure. Most amide protons showed different degrees of low field shifts with pressure, namely 0-0.2 ppm with an average of 0.051 ppm at 2000 bar, showing that they are involved in hydrogen bonding and that these hydrogen bonds are shortened by pressure by different degrees. The tendency was also confirmed that the chemical shifts of the amide protons exposed to the solvent (water) are more sensitive to pressure than those internally I lydrogen bonded with carbonyls. The pressure-induced shifts of the H-alpha signals of the residues in the beta-sheet showed a negative correlation with the 'folding' shifts (difference between the shift at 1 bar and that of a random coil), suggesting that the main-chain torsion angles of the beta-sheet are slightly altered by pressure. Significant pressure-induced shifts were also observed for the side-chain protons (but no larger than 10% of the 'folding' shifts), demonstrating that the tertiary structure of gurmarin is also affected by pressure. Finally, the linearity of the pressure-induced shifts suggests that the compressibility of gurmarin is invariant in the pressure range between 1 and 2000 bar.

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Documento generato il 20/09/20 alle ore 22:24:15