Organization of the MADS box from human SRF revealed by tyrosine perturbation
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F15%3A10314367" target="_blank" >RIV/00216208:11320/15:10314367 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1021/jp508897p" target="_blank" >http://dx.doi.org/10.1021/jp508897p</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/jp508897p" target="_blank" >10.1021/jp508897p</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Organization of the MADS box from human SRF revealed by tyrosine perturbation
Popis výsledku v původním jazyce
MADS box family transcription factors are involved in signal transduction and development control through DNA specific sequence recognition. The DNA binding domain of these proteins contains a conservative 55-60 amino acid sequence which defines the membership of this large family. Here we present a thorough study of the MADS segment of serum response factor (MADS(SRF)). Fluorescence, UV-absorption, and Raman spectroscopy studies were performed in order to disclose its behavior and basic functional properties in an aqueous environment. The secondary structure of MADS(SRF) estimated by analysis of Raman spectra and supported by CD has revealed only the C-terminal part as homologous with those of free core-SRF, while the N-terminal part has lost the stable a-helical structure found in both the free core-SRF and its specific complex with DNA. The three tyrosine residues of the MADS(SRF) were used as spectroscopic inner probes. The effect of environmental conditions, especially pH variatio
Název v anglickém jazyce
Organization of the MADS box from human SRF revealed by tyrosine perturbation
Popis výsledku anglicky
MADS box family transcription factors are involved in signal transduction and development control through DNA specific sequence recognition. The DNA binding domain of these proteins contains a conservative 55-60 amino acid sequence which defines the membership of this large family. Here we present a thorough study of the MADS segment of serum response factor (MADS(SRF)). Fluorescence, UV-absorption, and Raman spectroscopy studies were performed in order to disclose its behavior and basic functional properties in an aqueous environment. The secondary structure of MADS(SRF) estimated by analysis of Raman spectra and supported by CD has revealed only the C-terminal part as homologous with those of free core-SRF, while the N-terminal part has lost the stable a-helical structure found in both the free core-SRF and its specific complex with DNA. The three tyrosine residues of the MADS(SRF) were used as spectroscopic inner probes. The effect of environmental conditions, especially pH variatio
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
BO - Biofyzika
OECD FORD obor
—
Návaznosti výsledku
Projekt
<a href="/cs/project/GA202%2F09%2F0193" target="_blank" >GA202/09/0193: Vznik a dynamika strukturních motivů nukleových kyselin podílejících se na regulaci genové exprese</a><br>
Návaznosti
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2015
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Journal of Physical Chemistry B
ISSN
1520-6106
e-ISSN
—
Svazek periodika
119
Číslo periodika v rámci svazku
5
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
9
Strana od-do
1793-1801
Kód UT WoS článku
000349137000002
EID výsledku v databázi Scopus
2-s2.0-84922440730