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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 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Atomic force spectroscopic and SPR kinetic analysis of long circular and short ssDNA molecules interacting with single-stranded DNA-binding protein Author(s) Horáčková, V. (CZ)
Hlaváček, Antonín (UIACH-O) ORCID
Čundlerová, V. (CZ)
Pastucha, M. (CZ)
Skládal, P. (CZ)Number of authors 5 Source Title Monatshefte fur Chemie. - : Springer - ISSN 0026-9247
Roč. 148, č. 11 (2017), s. 2011-2018Number of pages 8 s. Publication form Print - P Language eng - English Country AT - Austria Keywords microscopy ; biology ; specificity ; surface Subject RIV CB - Analytical Chemistry, Separation OECD category Analytical chemistry Institutional support UIACH-O - RVO:68081715 UT WOS 000413626000015 EID SCOPUS 85028977895 DOI 10.1007/s00706-017-2022-9 Annotation 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. Workplace Institute of Analytical Chemistry Contact Iveta Drobníková, drobnikova@iach.cz, Tel.: 532 290 234 Year of Publishing 2018
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