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

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

Biopolymers

journal_title

Biopolymers

authors

Takekiyo T,Takeda N,Isogai Y,Kato M,Taniguchi Y

doi

10.1002/bip.20628

subject

Has Abstract

pub_date

2007-02-05 00:00:00

pages

185-8

issue

2

eissn

0006-3525

issn

1097-0282

journal_volume

85

pub_type

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