Macromolecular crowding increases structural content of folded proteins.

Abstract:

:Here we show that increased amount of secondary structure is acquired in the folded states of two structurally-different proteins (alpha-helical VlsE and alpha/beta flavodoxin) in the presence of macromolecular crowding agents. The structural content of flavodoxin and VlsE is enhanced by 33% and 70%, respectively, in 400 mg/ml Ficoll 70 (pH 7, 20 degrees C) and correlates with higher protein-thermal stability. In the same Ficoll range, there are only small effects on the unfolded-state structures of the proteins. This is the first in vitro assessment of crowding effects on the native-state structures at physiological conditions. Our findings imply that for proteins with low intrinsic stability, the functional structures in vivo may differ from those observed in dilute buffers.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Perham M,Stagg L,Wittung-Stafshede P

doi

10.1016/j.febslet.2007.09.049

subject

Has Abstract

pub_date

2007-10-30 00:00:00

pages

5065-9

issue

26

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(07)01031-9

journal_volume

581

pub_type

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