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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216224:14740/17:00095146

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Monatshefte fur Chemie

ISSN

0026-9247

e-ISSN

—

Svazek periodika

148

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

AT - Rakouská republika

Počet stran výsledku

8

Strana od-do

2011-2018

Kód UT WoS článku

000413626000015

EID výsledku v databázi Scopus

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