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Surface-attached protein can retain its native structure or undergo denaturation
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SYSNO ASEP 0328475 Document Type A - Abstract R&D Document Type The record was not marked in the RIV R&D Document Type Není vybrán druh dokumentu Title Surface-attached protein can retain its native structure or undergo denaturation Title Na povrch navázané bílkoviny mohou zůstávat v jejich nativní struktuře nebo podléhat denaturaci Author(s) Ostatná, Veronika (BFU-R) RID, ORCID
Paleček, Emil (BFU-R) RID, ORCIDSource Title Programme. - Sant Feliu de Guixols (Costa Brava), 2009
S. 1Number of pages 1 s. Action ESF-EMBO Symposium, Biological Surfaces and Interfaces Event date 27.06.2009-02.07.2009 VEvent location Sant Feliu de Guixols (Costa Brava) Country ES - Spain Event type EUR Language eng - English Country ES - Spain Keywords native and denatured BSA ; surface denaturation ; constant current chronopotentiometry Subject RIV BO - Biophysics R&D Projects GP202/07/P497 GA ČR - Czech Science Foundation (CSF) KJB100040901 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) LC06035 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z50040507 - BFU-R (2005-2011) AV0Z50040702 - BFU-R (2007-2013) Annotation Native and denatured states of bovine serum albumin were studied by constant current chronopotentiometry (CPS). Our recent results suggest that native protein structure can be retained at mercury electrodes during the CPS analysis. Recently we showed that in 50 mM sodium phosphate (pH 7) bovine serum albumin (BSA) and some other proteins were not significantly denatured at bare mercury electrode. at higher phosphate concentrations denaturation of BSA was detected on the electrode surface. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2010
Number of the records: 1