Pressure-tuning FT-IR spectroscopic study on the helix-coil transition of Ala-rich oligopeptide in aqueous solution.
Pressure-tuning FT-IR spectroscopic study on the helix-coil transition of Ala-rich oligopeptide in aqueous solution.
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DOI：
10.1016/j.bbapap.2005.02.014
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发表时间：
2005-06
期刊：
影响因子：
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通讯作者：
T. Takekiyo;A. Shimizu;Minoru Katō;Y. Taniguchi
中科院分区：
文献类型：
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作者：
T. Takekiyo;A. Shimizu;Minoru Katō;Y. Taniguchi
We investigated the effect of pressure on the helix–coil transition of an Ala-rich peptide (AK16: YGAAKAAAAKAAAAKA-NH2) in aqueous solution by FT-IR spectroscopy. The spectra of the amide I' region of AK16 in aqueous solution was decomposed into some component bands using a curve fitting method. The peak at around 1635 cm−1corresponding to the solvent exposed α-helix conformer increases with increasing pressures, while the peak at around 1655 cm−1corresponding to the random coil conformer decreases. From the pressure dependence of the band intensities, we determined the volume change from the α-helix to random coil conformers of AK16 to be +10.5±0.3 cm3/mol. The positive volume change is different from the negative volume change generally observed in the pressure denaturation of proteins.
