Pressure stability of the α-helix structure in a de novo designed protein (α-l-α)2 studied by FTIR spectroscopy
✍ Scribed by Takahiro Takekiyo; Naohiro Takeda; Yasuhiro Isogai; Minoru Kato; Yoshihiro Taniguchi
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2007
- Tongue
- English
- Weight
- 178 KB
- Volume
- 85
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The pressure‐induced structural changes of a de novo designed four‐helix bundle protein, (α‐l‐α)~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 α‐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 α‐helices of proteins. © 2006 Wiley Periodicals, Inc. Biopolymers 85:185–188, 2007.
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