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Macromolecular crowding increases structural content of folded proteins
Author(s) -
Perham Michael,
Stagg Loren,
Wittung-Stafshede Pernilla
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.09.049
Subject(s) - macromolecular crowding , ficoll , flavodoxin , chemistry , native state , macromolecule , biophysics , protein folding , protein secondary structure , protein stability , biochemistry , crowding , protein structure , in vitro , biology , enzyme , peripheral blood mononuclear cell , ferredoxin , neuroscience
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 400 mg/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.