Pressure stability of the alpha-helix structure in a de novo designed protein (alpha-l-alpha)(2) studied by FTIR spectroscopy.
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.
Takekiyo
Takahiro
T
Department of Applied Chemistry, Ritsumeikan University 1-1-1, Noji-higashi, Kusatsu, Shiga 525-8577, Japan.
Takeda
Naohiro
N
Isogai
Yasuhiro
Y
Kato
Minoru
M
Taniguchi
Yoshihiro
Y
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D011312:Pressure; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared
D011506:Proteins