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Surface-attached protein can retain its native structure or undergo denaturation

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, ORCID}
Source Title	Programme. - Sant Feliu de Guixols (Costa Brava), 2009 S. 1
Number 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