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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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manjavacasAlejandro Manjavacas Arévalo, a former PhD student at the IQFR, has been distinguished with the Young Investigator 2016 prize, granted jointly by the Spanish Physical Royal Society and the BBVA Foundation.
Dr Manjavaca, now at the New Mexico University (USA) as Associated Investigator, carried out his PhD research on “Light-matter interactions at nano-level” at this Institute, under the supervision of Prof. J. García Abajo. His doctoral dissertation, together with that of Dr. Luis Cerdán also from the IQFR, was distinguished with the “Premio Extraordinario 2012-2013” by the Complutense University of Madrid.

 

ERC alfonso saizAlfonso Saiz-Lopez, Research Scientist at CSIC and Head of the Link to the ERC press release in this Institute, has obtained an ERC Consolidator Grant 2016 funded with 2 M euros by the European Research Council for the 5-year project “Climate dimension of natural halogens in the Earth system: Past, present, future (CLIMAHAL)”.
Through an extremely competitive selection process, the ERC Consolidator Grants will fund 314 projects (24 in Spain) out of 2300 applications. The CLIMAHAL project will use a multidisciplinary approach including spectroscopic and kinetic methods, and theoretical modelling to determine for the first time how natural halogen molecules affect the climate of our planet in past, present and future scenarios.
The ERC Consolidator Grants open every year to support research of consolidated and exceptional scientists of any nationality and age. The ERC selects pioneering and high risk projects with ground-breaking ideas within their fields of research.

Link to the ERC press release

 

MRICOProfesor de Investigación del CSIC
Premio Nacional de Investigación, Enrique Moles (2003)
Medalla de Oro de la Real Sociedad española de Química (2002)

El 1 de diciembre de 2014 falleció Manuel Rico Sarompas. Licenciado y Doctor en Ciencias Químicas en la Universidad Complutense, realizó su postdoc en el Imperial College (Londres) especializándose en la técnica de Resonancia Magnética Nuclear (RMN). A su regreso se instaló en el Instituto Rocasolano del CSIC el primer espectrómetro de RMN de nuestro país, del que se hizo cargo. Sus primeras investigaciones en este campo se encuadraron en la obtención de parámetros magnéticos precisos y en el análisis conformacional de moléculas de "mediana complejidad", a la vez que hizo una amplia labor de difusión de la técnica y colaboró con diversos investigadores en la resolución de problemas de química orgánica y en la identificación de productos naturales. Pronto evolucionó a las aplicaciones biológicas de la RMN, en la que conseguiría valiosos resultados. A comienzos de los años 80 del siglo pasado demostró la presencia en solución acuosa de poblaciones significativas de hélice alfa en péptidos lineales. Estos estudios sobre el plegamiento autónomo de péptidos los completó con el análisis de otros elementos de estructura secundaria, horquillas y láminas beta, tanto con fragmentos de proteína como con péptidos de diseño.
Más tarde, en la década de los 90, determinó la primera estructura tridimensional de una proteína por RMN en nuestro país y la caracterización del plegamiento a nivel de residuo, poniendo de manifiesto la presencia de estructura residual en el estado desplegado en condiciones nativas. A estos estudios siguieron la resolución de un buen número de estructuras tridimensionales de proteínas y de ácidos nucleicos así como la caracterización biofísica de sistemas complejos utilizando fundamentalmente la técnica de RMN.


El trabajo de Manuel Rico se caracterizó por una clara visión de su campo y por el rigor y el tesón con el que abordaba sus investigaciones. Manolo tuvo mucho interés en que en su grupo se incluyeran y desarrollaran los últimos avances de la técnica de RMN y siempre peleó por conseguir la mejor instrumentación para el laboratorio de RMN del IQFR. Es de destacar su apuesta incondicional por los científicos jóvenes, aconsejándoles y animándoles a tomar riesgos y a apostar por su formación de postgrado. El resultado fue la formación de nuevos expertos y el crecimiento de los grupos de RMN en nuestro país.
Asimismo siempre se interesó por proporcionar a la comunidad científica foros de difusión y formación, participó en numerosos actos divulgativos y era miembro activo de varias sociedades científicas. Fue promotor de la Escuela de verano de RMN, de la que dirigió varias ediciones, por la que han pasado prácticamente todos los espectroscopistas de RMN del país. Fue el impulsor y creador de la Red Nacional de Estructura y Función de Proteínas que aúna a todos aquellos científicos que trabajan sobre esta temática en España, sirviendo de cauce de divulgación científica y de formación de estudiantes en el área.

 

"Frequenin/NCS-1 as a pharmacological target for synapse regulation in X-linked mental retardation and autism"

María José Sánchez Barrena

Miércoles 17 de diciembre

12:00 Salón de actos

Calendario de seminarios del curso 2014-2015 (Versión actualizada)

fig web1Plants have to endure adverse environmental conditions, among them, drought and salinity constrain agricultural productivity most dramatically. Many of the plant adaptive responses take place at cell membrane where it is required the regulation o a variety of ion channels and transporters. This adjusts the intracellular ion concentration necessary for cell live.  From a molecular point of view, the levels of abscisic acid (ABA) and calcium encode the information to orchestrate cell response to stress. We have discovered and characterized a new family of proteins, CAR for C2-domain ABA-related, that target ABA recognition machinery to the cell membrane. The joined structural and biochemical analyses has provided a working model that illustrates how CAR proteins anchor to plasma membrane and specifically bind the ABA receptors. As the activity of these proteins is dependent of calcium, they represent a central hub decoding ABA and calcium stimuli and provide a target for biotechnological work for the use of plants in our benefit.

C2-Domain Abscisic Acid-Related Proteins Mediate the Interaction of PYR/PYL/RCAR Abscisic Acid Receptors with the Plasma Membrane and Regulate Abscisic Acid Sensitivity in Arabidopsis

L. Rodriguez, M. Gonzalez-Guzmán, M. Díaz, A. Rodrigues, A.C. Izquierdo-Garcia, M. Peirats-Llobet, R. Antonia, D. Fernández, J.A. Márquez, J.M. Mulet, A. Albert and P.L. Rodríguez
The Plant Cell (2014) Advanced Online Publication (doi:10.1105/tpc.114.129973)

 

 

streptococcus pneumoniaeThe respiratory pathogen Streptococcus pneumoniae has evolved efficient mechanisms to resist oxidative stress conditions and to displace other bacteria in the nasopharynx. Here we characterize at physiological, functional and structural levels two novel surface-exposed thioredoxin-family lipoproteins, Etrx1 and Etrx2. The impact of both Etrx proteins and their redox partner methionine sulfoxide reductase SpMsrAB2 on pneumococcal pathogenesis was assessed in mouse virulence studies and phagocytosis assays. The results demonstrate that loss of function of either both Etrx proteins or SpMsrAB2 dramatically attenuated pneumococcal virulence in the acute mouse pneumonia model and that Etrx proteins compensate each other. The deficiency of Etrx proteins or SpMsrAB2 further enhanced bacterial uptake by macrophages, and accelerated pneumococcal killing by H2O2 or free methionine sulfoxides (MetSO). Moreover, the absence of both Etrx redox pathways provokes an accumulation of oxidized SpMsrAB2 in vivo. Taken together our results reveal insights into the role of two extracellular electron pathways required for reduction of SpMsrAB2 and surface-exposed MetSO. Identification of this system and its target proteins paves the way for the design of novel antimicrobials.

Reference:
Malek Saleh, Sergio G. Bartual, Mohammed R. Abdullah, Inga Jensch, Tauseef M. Asmat, Lothar Petruschka, Thomas Pribyl, Juan A. Hermoso* and Sven Hammerschmidt*
Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence
EMBO Molecular Medicine (2013) 5, 1852-1870  (doi:10.1002/emmm.201202435)

Referencia:

Malek Saleh, Sergio G. Bartual, Mohammed R. Abdullah, Inga Jensch, Tauseef M. Asmat, Lothar Petruschka, Thomas Pribyl, Juan A. Hermoso* and Sven Hammerschmidt*

Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence

EMBO Molecular Medicine (2013) 5, 1852-1870  (doi:10.1002/emmm.201202435)

We will have the traditional yearly meeting to briefly review 2013 at the main conference rooma t 13:00 and an informal lunch afterwards.

Cest-2923 figure-2

The alpha/beta hydrolase fold is one of the most versatile structures in the protein realm according to the diversity of sequences adopting such a three dimensional architecture. We found that the versatility of a canonical alpha/beta-hydrolase fold, particularly that of the carboxylesterase Cest-2923 from the lactic acid bacterium Lactobacillus plantarum WCFS1, also extends to its oligomeric behavior in solution. Thus, we discovered that Cest-2923 exhibits a pH-dependent pleomorphic behaviour in solution involving monomers, canonical dimers and tetramers. Whereas at neutral pH the system is mainly shifted to dimeric species, at acidic conditions tetrameric species predominate. Interestingly, despite that these tetramers result from the association of canonical dimers, as commonly found in many other carboxylesterases from the hormone-sensitive lipase family, they can be defined as “non canonical” since they represent a different association mode. The observed associative behaviour is consistent with different crystallographic results of Cest-2923 from structural genomics consortia. Finally, we benefit from the presence of sulphate or acetate molecules (depending on the crystal form analysed) in the close vicinity of the nucleophile Ser116, to identify interactions with the putative oxyanion hole and also to deduce the existence of hydrolytic activity within Cest-2923 crystals.

 

 

Reference:
Benavente R, Esteban-Torres M, Acebrón I, de Las Rivas B, Muñoz R, Alvarez Y, Mancheño JM. “Structure, biochemical characterization and analysis of the pleomorphism of carboxylesterase Cest-2923 from Lactobacillus plantarum WCFS1”. FEBS J. 2013 Oct 16. doi: 10.1111/febs.12569.