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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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December 2017
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Este Año el IQFR Duplica el Número de Actividades que Va a Realizar en el Marco de la Semana de la Ciencia.

Los días jueves 10 y viernes 11 de noviembre, tendremos días de puertas abiertas con charlas demostrativas seguidas con visitas a los laboratorios. El día 10, pondremos el foco sobre la investigación con una vertiente biológica, mientras el día 11 tendrá protagonismo la investigación con láseres, química atmosférica y nanomateriales. Estas actividades están principalmente dirigidas a los estudiantes de bachillerato.

**Se busca estudiantes de doctorando o técnicos jóvenes para servir como guías para las visitas a los laboratorios.**

Además, los días miércoles 16, jueves 17 y viernes 18 de noviembre, hemos programado tres encuentros y charlas con científicos sobre la resistencia de plantas a sequías, haciendo películas con electrones y amiloides respectivamente, desde las 18 - 19 horas de la tarde. Estas actividades son para una audiencia general, ¡QUE VENGA TODO EL MUNDO!

Tras la jubilación de Luis de la Vega, para facilitar las reservas a estas actividades, hemos puesto en marcha un Gestor:

reservas_sc16@iqfr.csic.es

Las escuelas o personas interesadas en asistir a las actividades deben escribir a esta dirección, indicando el nombre de la actividad que les interese, el nombre de la escuela, el número de estudiantes que quisieran acudir, y el nombre y un número de teléfono de la persona responsable.

Por otra parte, el día 8 de noviembre de 2016, habrá un taller de limpieza con láseres (5 sesiones de 45 minutos entra las 10 y 14 horas). Las personas interesadas en este taller deben contactar con Mohamed Oujja (m.oujja@iqfr.csic.es).

Por favor, tengan en cuenta que por las normas de la CAM, no podemos aceptar o gestionar reservas antes del 24 de octubre.

ParaBioF-small

Only 2% of the genome codes for proteins. What does the rest do? What is its structure? One of the most intriguing and unknown regions in the eukaryotic genome is the centromere. IQFR and CMBSO researchers have recently shown that centromeric sequences of organisms as distant in the evolutionary tree as fruit flies and humans are able to fold in vitro forming the same type of secondary structure, known as the “i-motif”. The presence of these structures in such distant organisms suggests that they may be involved in the structural organization of the centromere. If this were the case, the centromeric DNA could have been selected during evolution not for its primary sequence, but for its capability to form this non-canonical structure, the “i-motif”. 
 
This work is the result of a collaboration with our colleague and friend Alfredo Villasante, to whose memory it is dedicated.
 
M. Garavís, N. Escaja, V. Gabelica,  A. Villasante and C. González. Centromeric alpha-satellite DNA adopts dimeric i-motif structures capped by AT Hoogsteen base pairs. Chemistry-A Eur. J., 21, 9816-9824, 2015. doi: 10.1002/chem.201500448 (artículo del mes SBE, junio 2015)
 
M. Garavís, M. Méndez-Lago, V. Gabelica, S. L. Whitehead  G. González, and A. Villasante. The structure of an endogenous Drosophila centromere reveals the prevalence of tandemly repeated sequences able to form i-motifs. Sci. Rep., 5, 13307, 2015. doi: 10.1038/srep13307
 
 

nanoestructuras-ferrita

Ultrathin islands of up to 100 μm2 with atomically flat surfaces and free from antiphase boundaries are developed. The extremely low defect concentration leads to a robust magnetic order, even for thicknesses below 1 nm, and exceptionally large magnetic domains. This approach allows the evaluation of the influence of specific extrinsic effects on domain wall pinning. The work has been performed by researchers of the Instituto de Quimica-Física "Rocasolano" and other CSIC institutes (ICV, ICMM) in collaboration with Alba synchrotron scientists.

 

L. Martín-García, A. Quesada, C. Munuera, J.F. Fernández, M. García-Hernández, M. Foerster, L. Aballe, J. de la Figuera. Atomically flat ultrathin cobalt ferrite islands.Advanced Materials. DOI: 10.1002/adma.201502799

 

 

arriba

abajo

Scientists from the Department of Biophysical Chemistry discovered novel water-soluble oxocines and azocines that produce blue fluorescence with 100% quantum yield. These molecules are the main product of a new fluorogenic reaction that converts non-emitting biocompounds as L-DOPA, dopamine, hydroxytyrosol, etc. into useful photostable fluorophores. The new molecular structures contain the rare four-ring chromophore which originated the first written account of fluorescence emission in 1565 (Acuña et al. Org. Lett. 2009, 11, 3020). At that time, the medical doctor N. Monardes from Sevilla reported the unusual blue “color” (fluorescence) of the infusion of a medicinal wood widely used in preHispanic Aztec culture.

 

Reference:

Synthesis and photophysics of novel biocompatible fluorescent oxocines and azocines in aqueous solution.

A.Ulises Acuña, Mónica Älvarez-Pérez, Marta Liras, Pedro B. Coto and Francisco Amat-Guerri.

Phys. Chem. Chem. Phys. Sept. 2013 (DOI: 10:1039/c3cp52228h)

 

nap2pNab2p is an essential protein involved in mRNP (messenger ribonucleoprotein particles) formation and export in Saccharomyces cerevisiae. Its specific poly(A) RNA recognition ability resides on a region containing 7 CCCH-type zinc finger domains, of which, the last three zinc finger structure was previously known. In our group, we have solved the NMR structure of the first 4 zinc fingers that show novel elements in their fold. The first two zinc fingers (Zf1 and Zf2) form a compact tandem stabilized by a new -helix contacting both. Zf3 and Zf4 form a second tandem in which the metallic centres associate in a singular symmetric way with mutual recognition of the Zn2+ coordinating histidines. NMR, fluorescence anisotropy and mutagenesis studies identify the -helix in the first tandem and the exposed surface of Zf3 as the RNA binding interface. Our results allow us to propose a recognition model where Nab2p Zf1-4 cooperates with Nab2p Zf5-7 to reconstitute the poly(A) binding profile of the full-length protein.

 

Reference

Two Singular Types of CCCH Tandem Zinc Finger in Nab2p Contribute to Polyadenosine RNA Recognition.

Martínez-Lumbreras S1,3, Santiveri CM2,3, Mirassou Y1, Zorrilla S1,2, Pérez-Cañadillas JM1*.

Structure. 2013 Aug 28. doi: 10.1016/j.str.2013.07.019.

1 IQFR-CSIC; 2 CIB-CSIC; 3 equal contribution;*corresponding author

 

Figure-4A small

Bacterial cell wall is a polymer of considerable complexity that is in constant equilibrium between synthesis and recycling. AmpDh3 is a periplasmic zinc protease of Pseudomonas aeruginosa, which is intimately involved in cell-wall remodeling. In this report we document the reactions that this enzyme performs on the cell wall, which hydrolyze the peptide stems from the peptidoglycan, the major constituent of the cell wall. We document that the majority of the reactions of this enzyme takes place on the polymeric insoluble portion of the cell wall, as opposed to the fraction that is released from it. We show that AmpDh3 is tetrameric both in crystals and in solution. Based on the X-ray structures of the enzyme in complex with two synthetic cell-wall-based ligands, we present for the first time a model for a multivalent anchoring of AmpDh3 onto the cell wall, which lends itself to its processive remodeling.

 

 

      Reference:

Lee, M.; Artola-Recolons, C.; Carrasco-López, C.; Martínez-Caballero, S.; Hesek, D.; Spink, E.; Lastochkin, E.; Zhang, W.; Hellman, L.; Boggess, B.; Hermoso*, J.; Mobashery*, S.

      Cell-Wall Remodeling by the Zinc-Protease AmpDh3 from Pseudomonas aeruginosa

      J. Am. Chem. Soc. 2013; 12605-12607.