Pressure-tuning FT-IR spectroscopic study on the helix-coil transition of Ala-rich oligopeptide in aqueous solution

被引：34

作者：

Takekiyo, T

Shimizu, A

Kato, M

Taniguchi, Y ^{[1
]}

机构：

[1] Ritsumeikan Univ, Dept Appl Chem, Shiga 5258577, Japan

[2] Soka Univ, Fac Engn, Dept Bioengn, Tokyo 1928577, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2005年 / 1750卷 / 01期

关键词：

Ala-rich peptide; pressure effect; helix-coil transition; partial molar volume; FT-TR spectroscopy;

D O I：

10.1016/j.bbapap.2005.02.014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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(-1) corresponding to the solvent exposed a-helix conformer increases with increasing pressures, while the peak at around 1655 cm(-1) corresponding to the random coil conformer decreases. From the pressure dependence of the band intensities, we determined the volume change from the a-helix to random coil conformers of AK(16) to be + 10.5 +/- 0.3 cm(3)/mol. The positive volume change is different from the negative volume change generally observed in the pressure denaturation of proteins. (c) 2005 Elsevier B.V. All rights reserved.

引用

页码：1 / 4

页数：4

共 20 条

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