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Biophysical characterization of recombinant human ameloblastin
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SYSNO ASEP 0390090 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Biophysical characterization of recombinant human ameloblastin Author(s) Wald, Tomáš (MBU-M) RID
Bednárová, Lucie (UOCHB-X) RID, ORCID
Osička, Radim (MBU-M) RID, ORCID
Pachl, Petr (UOCHB-X) RID, ORCID
Šulc, Miroslav (MBU-M) RID, ORCID
Lyngstadaas, S. P. (NO)
Slabý, Ivan (BTO-N)
Vondrášek, Jiří (BTO-N)Source Title European Journal of Oral Sciences. - : Wiley - ISSN 0909-8836
Roč. 119, č. 1 (2011), s. 261-269Number of pages 9 s. Language eng - English Country US - United States Keywords circular dichroism spectroscopy ; dynamic light scattering ; enamel matrix protein Subject RIV EE - Microbiology, Virology R&D Projects GAP302/10/0427 GA ČR - Czech Science Foundation (CSF) LC512 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) UT WOS 000299070300039 DOI 10.1111/j.1600-0722.2011.00913.x Annotation Ameloblastin (AMBN) is a protein expressed mainly during dental hard tissue development. Biochemically, it is classified as an intrinsically disordered protein (IDP). Its biological role remains largely unknown; however, the question of AMBN function will undoubtedly be connected to its structural properties and its potential for protein-protein and protein-cell interactions. A basic biophysical characterization of human recombinant ameloblastin (hrAMBN) and its N- and C-terminal domains by means of circular dichroism spectroscopy and dynamic light scattering showed that under physiological conditions ameloblastin is an IDP with a prevalent polyproline-II (PPII) conformation. Both the N- and C-terminal polypeptides, when expressed independently, showed different structural preferences upon heating as well as different behaviour in the presence of trifluoroethanol and CaCl(2) salt. The N-terminal peptide showed a more ordered structure with a strong tendency to adopt a helical conformation upon the addition of trifluorethanol, whereas the C-terminal domain seemed to be primarily responsible for the structural disorder of the entire AMBN molecule Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2013
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