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- W2050455962 abstract "The conformational stability of [Leu]5-enkephalin,Tyr-Gly-Gly-Phe-Leu, in water have been investigated under high pressure by FTIR spectroscopy. Three peaks at 1638, 1650, and 1680 cm−1 were determined by second derivative FTIR spectra in the amide I' region of [Leu]5-enkephalin. The peaks at 1637 and 1680 cm−1 are assigned to the β-strand and turn structures, respectively. These peaks mean that [Leu]5-enkephalin takes a β-hairpin-like structure in water. Moreover, the absorbance at 1638 cm−1 increases with increasing pressure, and this change shows a sigmoidal curve. Thus, we concluded that [Leu]5-enkephalin has the β-hairpin-like and disordered structures in water. From the FTIR profile at high pressures, the β-hairpin-like structure of [Leu]5-enkephalin is stabilized by a high pressures. Our result shows that the folded structures such as α-helix and β-hairpin structures of short peptide such as [Leu]5-enkephalin are stabilized at high pressures." @default.
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- W2050455962 date "2010-03-01" @default.
- W2050455962 modified "2023-10-18" @default.
- W2050455962 title "Pressure effect on the conformational equilibrium of [Leu]5-enkephalin in water" @default.
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- W2050455962 doi "https://doi.org/10.1088/1742-6596/215/1/012153" @default.
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