Please use this identifier to cite or link to this item:
|Title:||Biophysical characterization of Gir2, a highly acidic protein of Saccharomyces cerevisiae with anomalous electrophoretic behavior|
|Authors:||Alves, V. S.|
Pimenta, D. C.
Castilho, B. A.
Universidade Federal de São Paulo (UNIFESP)
Ctr Toxincol Aplicada
|Citation:||Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 314, n. 1, p. 229-234, 2004.|
|Abstract:||Gir2 is an uncharacterized protein of Saccharomyces cerevisiae, containing a RWD/GI domain. in this work, we report the biophysical characterization of Gir2. His-tagged Gir2, expressed and purified from Escherichia coli, showed an abnormally slow migration on SDS-PAGE. the yeast expressed protein behaves similarly. Using mass spectrometry and peptide mass fingerprinting we demonstrated that the protein has the expected molecular mass (34 kDa). EDC modification of carboxylate groups reverted the anomalous migration on SDS-PAGE. Size exclusion chromatography showed that Gir2 has a Stokes radius larger than expected. Gir2 is thermostable and lacks extensive structure, as determined by CD analysis. Based on these findings, we suggest that Gir2 is a representative of the growing group of natively unfolded proteins. (C) 2003 Elsevier Inc. All rights reserved.|
|Appears in Collections:||Em verificação - Geral|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.