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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

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 

 

“The multiple faces of RNA binding proteins”

May 29th 2013

May 22th, 10:00h. General meeting of the institute for the presentación of Dr. Juan de la Figuera as candidate for director.

Imagen Tesis ReduThe Thesis entitled Electrocatalysis and surface nanostructuring: atomic ensemble effects and non-covalent interactions, whose author is Dr. María Escudero Escribano, and which was developed at the Institute of Physical Chemistry "Rocasolano" under the supervision of Dr. Angel Cuesta Ciscar, has received the Prize to the Best PhD Thesis in the Region of Madrid in the course 2011-2012, awarded by the Madrid Chapter of the Spanish Royal Society of Chemistry (RSEQ). The research was focused on the study of the role of geometric atomic ensembles in electrocatalysis, and on the fabrication of surface nanostructures guided by a self-ordered molecular pattern, namely cyanide-modified Pt(111). The Thesis can be downloaded from Digital CSIC (http://hdl.handle.net/10261/42378).

 

Suc2 octa webScientists from IQFR have revealed the structure of the Saccharomyces invertase, a highly interesting enzyme for Biotechnology and a classical model used in early biochemical studies. In the study have participated scientists from IATA (CSIC).
Invertases catalyze the hydrolysis of the disaccharide sucrose into glucose and fructose, being key enzymes in the metabolism of plants and microorganisms. Besides its historic relevance, Saccharomyces invertase is one of the most widely used enzymes in food industry, and in the fermentation of cane molasses into ethanol. A new emerging application is the synthesis of prebiotics (FOS) for use in functional foods and pharmaceuticals.

 

Reference: Journal of Biological Chemistry (2013) 288, 9755- 9766 (doi:10.1074/jbc.M112.446435)
Three-dimensional structure of Saccharomyces invertase. Role of a non-catalytic domain in oligomerization and substrate specificity. http://www.jbc.org/content/288/14/9755#fn-9
MA Sainz-Polo. M Ramírez, A Lafraya, B González, J Marín-Navarro, J Polaina, J Sanz-Aparicio.


Its structural analysis has shown a sophisticated molecular architecture with a peculiar monomer assembly, unique to this enzyme within its family, which regulates its specificity. This assemblage is similar to the interactions that form b-amiloids, and is mediated by the non-catalytic domain. Therefore, our results highlight the role of the non-catalytic domains in fine-tuning substrate specificity and supplement our knowledge into the structural features that rule modularity, a central feature within carbohydrate-active enzymes.

Press note.

 

Streptococcus pneumoniae surface-exposed thioredoxin-like proteins that are involved in defence against oxidative stress

May 22th 2013