Atomic force spectroscopic and SPR kinetic analysis of long circular and short ssDNA molecules interacting with single-stranded DNA-binding protein

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081715%3A_____%2F17%3A00481141" target="_blank" >RIV/68081715:_____/17:00481141 - isvavai.cz</a>

Alternative codes found

RIV/00216224:14740/17:00095146

Result on the web

<a href="http://dx.doi.org/10.1007/s00706-017-2022-9" target="_blank" >http://dx.doi.org/10.1007/s00706-017-2022-9</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00706-017-2022-9" target="_blank" >10.1007/s00706-017-2022-9</a>

Result language

angličtina

Original language name

Atomic force spectroscopic and SPR kinetic analysis of long circular and short ssDNA molecules interacting with single-stranded DNA-binding protein

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10406 - Analytical chemistry

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Monatshefte fur Chemie

ISSN

0026-9247

e-ISSN

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Volume of the periodical

148

Issue of the periodical within the volume

11

Country of publishing house

AT - AUSTRIA

Number of pages

8

Pages from-to

2011-2018

UT code for WoS article

000413626000015

EID of the result in the Scopus database

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