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@article{1394951,
author = {Horáčková, Veronika and Hlaváček, Antonín and Čunderlová, Veronika and Pastucha, Matěj and Skládal, Petr},
article_location = {Wien},
article_number = {11},
doi = {http://dx.doi.org/10.1007/s00706-017-2022-9},
keywords = {Atomic force microscopy; Surface plasmon resonance; Electrophoretic mobility shift assay; ssDNA-SSB protein complex},
language = {eng},
issn = {0026-9247},
journal = {Monatshefte fur Chemie},
title = {Atomic force spectroscopic and SPR kinetic analysis of long circular and short ssDNA molecules interacting with single-stranded DNA-binding protein},
url = {https://link.springer.com/article/10.1007/s00706-017-2022-9},
volume = {148},
year = {2017}
}
TY - JOUR
ID - 1394951
AU - Horáčková, Veronika - Hlaváček, Antonín - Čunderlová, Veronika - Pastucha, Matěj - Skládal, Petr
PY - 2017
TI - Atomic force spectroscopic and SPR kinetic analysis of long circular and short ssDNA molecules interacting with single-stranded DNA-binding protein
JF - Monatshefte fur Chemie
VL - 148
IS - 11
SP - 2011-2018
EP - 2011-2018
PB - Springer-Verlag
SN - 00269247
KW - Atomic force microscopy
KW - Surface plasmon resonance
KW - Electrophoretic mobility shift assay
KW - ssDNA-SSB protein complex
UR - https://link.springer.com/article/10.1007/s00706-017-2022-9
L2 - https://link.springer.com/article/10.1007/s00706-017-2022-9
N2 - 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.
ER -
HORÁČKOVÁ, Veronika, Antonín HLAVÁČEK, Veronika ČUNDERLOVÁ, Matěj PASTUCHA and Petr SKLÁDAL. Atomic force spectroscopic and SPR kinetic analysis of long circular and short ssDNA molecules interacting with single-stranded DNA-binding protein. \textit{Monatshefte fur Chemie}. Wien: Springer-Verlag, 2017, vol.~148, No~11, p.~2011-2018. ISSN~0026-9247. Available from: https://dx.doi.org/10.1007/s00706-017-2022-9.
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