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 Lettjournal_title
FEBS lettersauthors
Perham M,Stagg L,Wittung-Stafshede Pdoi
10.1016/j.febslet.2007.09.049subject
Has Abstractpub_date
2007-10-30 00:00:00pages
5065-9issue
26eissn
0014-5793issn
1873-3468pii
S0014-5793(07)01031-9journal_volume
581pub_type
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