Počet záznamů: 1
Atomic force spectroscopic and SPR kinetic analysis of long circular and short ssDNA molecules interacting with single-stranded DNA-binding protein
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SYSNO ASEP 0481141 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Atomic force spectroscopic and SPR kinetic analysis of long circular and short ssDNA molecules interacting with single-stranded DNA-binding protein Tvůrce(i) Horáčková, V. (CZ)
Hlaváček, Antonín (UIACH-O) ORCID
Čundlerová, V. (CZ)
Pastucha, M. (CZ)
Skládal, P. (CZ)Celkový počet autorů 5 Zdroj.dok. Monatshefte fur Chemie. - : Springer - ISSN 0026-9247
Roč. 148, č. 11 (2017), s. 2011-2018Poč.str. 8 s. Forma vydání Tištěná - P Jazyk dok. eng - angličtina Země vyd. AT - Rakousko Klíč. slova microscopy ; biology ; specificity ; surface Vědní obor RIV CB - Analytická chemie, separace Obor OECD Analytical chemistry Institucionální podpora UIACH-O - RVO:68081715 UT WOS 000413626000015 EID SCOPUS 85028977895 DOI 10.1007/s00706-017-2022-9 Anotace Regulation of cellular processes and biochemical pathways would not be possible without formation of specific non-covalent complexes between nucleic acids and proteins. Single-stranded DNA-binding proteins have a high affinity for ssDNA and this interaction plays a crucial role in the control of DNA replication, recombination, transcription, translation, and repair. Characterization of the DNA-protein interactions would improve the information about abnormal cells and provide a better understanding of tumor growth, its prevention, and medical treatment. The interaction between the ssDNA-binding protein from E. coli with two ssDNA molecules (either M13mp18, 7249 bases, or a short 10 base oligonucleotide) was analyzed using atomic force microscopy providing images of the formed complexes on mica. The corresponding binding forces were determined using force spectroscopy using cantilever tips modified with ssDNA. The interactions were also characterized using the surface plasmon resonance (Biacore) providing reference data on kinetics in real time. The data from different methods were critically evaluated and discussed with respect to correlation of the single- (force spectroscopy) and multi-molecular (biosensor kinetics) results. Pracoviště Ústav analytické chemie Kontakt Iveta Drobníková, drobnikova@iach.cz, Tel.: 532 290 234 Rok sběru 2018
Počet záznamů: 1