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Updated: Jul 18, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
Pressure stability of the alpha-helix structure in a de novo designed protein (alpha-l-alpha)(2) studied by FTIR
Takahiro Takekiyo1, Naohiro Takeda, Yasuhiro Isogai
1Department of Applied Chemistry, Ritsumeikan University 1-1-1, Noji-higashi, Kusatsu, Shiga 525-8577, Japan.
Abstract:
The pressure-induced structural changes of a de novo designed four-helix bundle protein, (alpha-l-alpha)(2), in aqueous solution have been investigated by FTIR spectroscopy. Changes in the amide I' band intensity show that pressure induces disruption of tertiary interactions and stabilizes the solvated alpha-helical form. This may suggest that the exposure of the hydrophobic core to the solvent by pressure is not a sufficient condition for pressure-induced unfolding of the alpha-helices of proteins.
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