The C-Terminal Segment of Yeast BMH Proteins Exhibits Different Structure Compared to Other 14-3-3 Protein Isoforms

0344035 - FGÚ 2011 RIV US eng J - Článek v odborném periodiku
Veisová, Dana - Řežábková, L. - Štěpánek, M. - Novotná, P. - Herman, P. - Večeř, J. - Obšil, T. - Obšilová, Veronika
The C-Terminal Segment of Yeast BMH Proteins Exhibits Different Structure Compared to Other 14-3-3 Protein Isoforms.
Biochemistry. Roč. 49, č. 18 (2010), s. 3853-3861. ISSN 0006-2960
Grant CEP: GA AV ČR(CZ) IAA501110801; GA MŠMT(CZ) LC554
Výzkumný záměr: CEZ:AV0Z50110509
Klíčová slova: yeast BMH proteins * sedimentation equilibrium and velocity measurements * dynamic light scattering
Kód oboru RIV: BO - Biofyzika
Impakt faktor: 3.226, rok: 2010

We have investigated the conformational behavior of the C-terminal segment of BMH proteins using the array of biophysical techniques: dynamic light scattering, sedimentation velocity, sedimentation equilibrium, time-resolved fluorescence anisotropy decay, and size exclusion chromatography measurements. We showed that the C-terminal segment of BMH proteins adopts a widely opened and extended conformation that makes difficult its folding into the ligand binding groove, thus increasing the apparent molecular size. It seems, therefore, that the C-terminal segment of BMH proteins does not function as an autoinhibitor
Trvalý link: http://hdl.handle.net/11104/0186358