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The C-Terminal Segment of Yeast BMH Proteins Exhibits Different Structure Compared to Other 14-3-3 Protein Isoforms
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SYSNO ASEP 0344035 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The C-Terminal Segment of Yeast BMH Proteins Exhibits Different Structure Compared to Other 14-3-3 Protein Isoforms Author(s) Veisová, Dana (FGU-C)
Řežábková, L. (CZ)
Štěpánek, M. (CZ)
Novotná, P. (CZ)
Herman, P. (CZ)
Večeř, J. (CZ)
Obšil, T. (CZ)
Obšilová, Veronika (FGU-C) RID, ORCID, SAISource Title Biochemistry. - : American Chemical Society - ISSN 0006-2960
Roč. 49, č. 18 (2010), s. 3853-3861Number of pages 9 s. Language eng - English Country US - United States Keywords yeast BMH proteins ; sedimentation equilibrium and velocity measurements ; dynamic light scattering Subject RIV BO - Biophysics R&D Projects IAA501110801 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) LC554 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z50110509 - FGU-C (2005-2011) UT WOS 000277212400008 DOI 10.1021/bi100273k Annotation 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 Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2011
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