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- Title
Macromolecular crowding increases structural content of folded proteins
- Authors
Perham, Michael; Stagg, Loren; Wittung-Stafshede, Pernilla
- Abstract
Abstract: Here we show that increased amount of secondary structure is acquired in the folded states of two structurally-different proteins (α-helical VlsE and α/β flavodoxin) in the presence of macromolecular crowding agents. The structural content of flavodoxin and VlsE is enhanced by 33% and 70%, respectively, in 400mg/ml Ficoll 70 (pH 7, 20°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.
- Subjects
PROTEINS; MACROMOLECULES; STABILITY (Mechanics); BIOMACROMOLECULES
- Publication
FEBS Letters, 2007, Vol 581, Issue 26, p5065
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2007.09.049