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In its 85-year story, the mission of our institute has been to carry out excellence research in fundamental and applied physical chemistry, contributing to the scientific training of several generations of researchers at the highest level. Our vision is to be an international reference in multidisciplinary research focused on the resolution of the present challenges of our society in the fields of health, biotechnology, new materials, and environment.

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News

"Actividades de investigación en el Grupo de Química Atmosférica y Clima"

Thursday 20th June 2013

12:00 Salón de Actos de IQFR

"Estudios mediante RMN de la estructura y estabilidad de ácidos nucleicos con furanosas modificada"

Tuesday 18th June  2013

12:00 Salón de Actos del IQRF

"From Bayes (to electrons to proteins) to therapies"

Wednesday 19th, 2013

12:00 Salón de Actos

Modelado y simulación de procesos de adsorción en arcillas con pilares intercalados

12:00 Salón de Actos

Wednesday, June 12th 2013

figura webScientists from IQFR have revealed the inhibition mechanism of UDG, a key enzyme for DNA repair. The work has been developed in collaboration with scientists from CBMSO (CSIC-UAM).

 

UDG is the first enzyme acting in a specific DNA repair pathway, called BER, where it detects uracil in DNA. Once detected, uracil is removed and subsequent enzymes within the BER pathway continue the process. Several proteins have been identified capable to inhibit UDG, among them p56 encoded by different phages probably as a defence mechanism.

 

p56 is a DNA mimic protein that blocks the UDG active site. The structure of the complex showed a specific recognition pattern between UDG and p56 that explains the lack of cross-reactivity among p566 and other DNA binding proteins. Therefore, our results shed light onto the UDG-blocking mechanism used by some viruses to proliferate into the host cell. Moreover, they pave the way to the potential use of p56 as antiviral agent against some infectious caused by herpes and poxvirus.

Publication:
José Ignacio Baños-Sanz, Laura Mojardín, Julia Sanz-Aparicio, José M. Lázaro, Laurentino Villar, Gemma Serrano-Heras, Beatriz González*, and Margarita Salas*.
Crystal structure and functional insights into uracil-DNA glycosylase inhibition by phage ϕ29 DNA mimic protein p56
Nucl. Acids Res. 2013 doi:10.1093/nar/gkt395

 

Wednesday June 12th 2013

"Nonlocal effects in plasmonic devices: Exploring the quantum regime with the classical hydrodynamic approach"

June 5th 2013

2013 JACS Davalos Researchers from IQFR (J. Dávalos, A. Guerrero, J. Gonzalez, A. Chana) in collaboration of Prof. T. Baer (University of North Carolina-USA) have determined the acidity GA -in the gas phase- of the hydroxyl and carboxyl local groups of the hydroxycinnamic acids, applying the kinetic method (EKM) in a mass spectrometer with electrospray (ESI)-source. Hydroxycinnamic acids are natural compounds found in several biological sources mostly in the plant kingdom either as esters of organic acids or glycosides, bound to proteins or as free acids.

The most important contribution of this work has been to show that is possible to determine gas-phase acidities (GAs) or basicities (GBs) of different deprotonation or protonation sites of a same molecule, only by a careful control of the ESI-experimental conditions; since the measurement of GA or GB of monofunctional molecules not offer a new scientific challenge.

This work opens the implementation of new experimental methodologies (e.g. using ESI-MS) to extract and quantify reliable thermodynamic properties, such as GA or GB, of different local groups within a multifunctional molecule.

 

Reference: Gas phase acidity measurement of local acidic groups in multifunctional species: Controlling the binding sites in hydroxycinnamic acids, A. Guerrero, T. Baer, A. Chana, F.J. González, and J.Z. Dávalos, J. Amer. Chem. Soc. (2013) DOI:10.1021/ja400571r 

 

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