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.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Takekiyo T,Takeda N,Isogai Y,Kato M,Taniguchi Ydoi
10.1002/bip.20628subject
Has Abstractpub_date
2007-02-05 00:00:00pages
185-8issue
2eissn
0006-3525issn
1097-0282journal_volume
85pub_type
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