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

✍ Scribed by Takahiro Takekiyo; Akio Shimizu; Minoru Kato; Yoshihiro Taniguchi

• Publisher: Elsevier Science
• Year: 2005
• Tongue: English
• Weight: 142 KB
• Volume: 1750
• Category: Article
• ISSN: 1570-9639
• DOI: 10.1016/j.bbapap.2005.02.014

✦ Synopsis

We investigated the effect of pressure on the helix-coil transition of an Ala-rich peptide (AK16: YGAAKAAAAKAAAAKA-NH(2)) 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 alpha-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 alpha-helix to random coil conformers of AK16 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.