Pressure stability of the alpha -helix structure in a de novo designed protein ( alpha -l- alpha ) sub(2) studied by FTIR spectroscopy

The pressure-induced structural changes of a de novo designed four-helix bundle protein, ( alpha -l- alpha ) sub(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 th...

Full description

Saved in:
Bibliographic Details
Published in:Biopolymers 2007-01, Vol.85 (2), p.185-188
Main Authors: Takekiyo, Takahiro, Takeda, Naohiro, Isogai, Yasuhiro, Kato, Minoru, Taniguchi, Yoshihiro
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The pressure-induced structural changes of a de novo designed four-helix bundle protein, ( alpha -l- alpha ) sub(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.
ISSN:0006-3525
1097-0282
DOI:10.1002/bip.20628