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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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Coincident with the anniversary of the demise of our colleague Noé García Almarza, Soft Matter has published one of his last research studies that has also been highlighted in the Inside Front Cover of the aforementioned journal.

Simposio Julio Palacios

Under the auspices of the "Julio Palacios" Chair, created by the Spanish National Research Council (CSIC) in 2015, the First "Julio Palacios" International Symposium will take place between 20th and 22nd July 2016 in the city of La Coruña (Spain). The symposium, of broad interest and with a multidisciplinary character, is intended for a general public and especially for university students. The main goal is to provide a meeting point and informative debate on the frontiers of modern science. Registration is free up to the venue capacity. Among the speakers, we can highlight Ignacio Cirac, a renowned theoretical physicist, Douglas Klein, a world-wide expert in mathematical chemistry, Ángel Carracedo, an expert in genomic medicine, or Harald Helfgott, the mathematician who recently proved the ternary Goldbach conjecture, an unsolved problem dated on 1742.

Julio Palacios (1891-1970), a physicist and Professor from The Central University in Madrid (nowadays Complutense University) and researcher in the Spanish National Research Council (CSIC), can be considered among the most relevant Spanish scientists. He was member of different institutions: President of the Spanish Royal Society of Physics and Chemistry, President of the Royal Academy of Exact, Physical and Natural Sciences and member of the Spanish Royal Academy (Spanish language) and of the Royal Academy of Medicine, among others.

More information in:


MCS2016We are pleased to announce the sixth edition of the Macromolecular Crystallography School - MCS2016, to be held at the CBE (Department of Crystallography and Structural Biology) of the Institute of Physical-Chemistry "Rocasolano", CSIC (Spanish National Research Council), in Madrid, May 2016.

The MCS2016 is directed to 25 graduate students and/or researchers with some previous expertise in crystallography which need a deeper insight into most advanced crystallographic techniques to carry out their research projects. The school program covers aspects such as sample preparation, phasing, model building, crystallographic refinement, validation, and analysis of the structural results




HBC revised-MMRThe discovery of stable amyloids composed solely of polar residues surprised scholars who believed that protein conformational stability is chiefly due to the hydrophobic effect. These amyloids, rich in Asn and Gln residues, form extensive hydrogen bonding networks. When aligned, hydrogen bond networks are strengthened due to cooperative effects arising from hyperpolarization. In this work, Density Functional Theory and Natural Bonding Orbital analysis were applied to study a series of polar and hydrophobic peptides in amyloid-like oligomers of different sizes and revealed that hydrogen bond networks formed by Asn and Gln side chains experience a distinct class of cooperativity that strengthens them significantly relative to main chain hydrogen bond networks. These computational results were corroborated experimentally utilizing recognition by amyloid specific molecular probes, nuclear magnetic resonance spectroscopy and experimental electric conductivity measurements on Asn/Gln-rich and hydrophobic peptides. On the basis of these findings, approaches to selectively inhibit the formation of polar versus hydrophobic amyloids can now be devised.

The figure shows a schematic representation of the delocalized electron density (blue shading) in the H-bond networks formed by Asn side chains (left) and the peptide backbone (right).

Miguel Mompeán, Aurora Nogales, Tiberio A. Ezquerra & Douglas V. Laurents ( "Complex System Assembly Underlies a Two-Tiered Model of Highly Delocalized Electrons" J. Phys. Chem. Lett. (2016) 7(10): 1859-1864.


Reunión del Claustro Científico

Viernes 29 de mayo de 2015

10:00, salón de actos

"Glicomica funcional: hacia la aplicación biomédica"

Ioanna Kalograiaki

Miércoles 3 de junio

12:00, salón de actos

Conferenciante: Profesor Neil L. Allan (Universidad de Bristol, Reino Unido)
Fecha: Viernes, 29 de Mayo de 2015
Hora: 12:00 horas
Lugar: Salón de Actos del IQFR (CSIC). C/Serrano, 119. Madrid

"Current state of Fluorescence Micro-Spectroscopy Methods at the IQFR: Living cells and in vitro applications"

María Pilar Lillo

Miércoles 20 de mayo

Salón de actos, 12:00

"Amyloids: Friends or Foes"

Douglas Laurents

Miércoles 13 de mayo

Salón de Actos, 11:00 (Atención al cambio de hora)

"Mecanismos de Reconocimiento de Proteínas +TIPS (Tip Interacting Proteins)"

Viernes 6 de junio

Aula 300, 12:00

"Búsqueda de nuevas léctinas fúngicas con estructura trébol beta: desarrollo de nuevas aplicaciones biotecnológicas"

Jueves 22 de Mayo

Salón de Actos 12:00

Universidad Texas A&M

“Entropy vs. Mixing: What Determines Complexity”

Martes 27 de Mayo

Salón de actos, 12:00

xtal libroM. Martínez-Ripoll, J.A. Hermoso & Armando Albert (coord.), CSIC-Catarata (2014), 196 pp., ISBN: 978-84-00-09800-1.

Un libro de divulgación científica en el contexto del Año Internacional de la Cristalografía 2014.

Se puede encontrar un ejemplar en la biblioteca del IQFR.

A book for scientific dissemination in the context of the International Year of Crystallography 2014 (IYCr2014).

You may find a copy at the IQFR library.


    Separation of daughter cells during bacterial cell division requires that the septal cross wall be split by peptidoglycan hydrolases. In Streptococcus pneumoniae an essential protein termed PcsB is predicted to perform this critical operation. Recent evidence shows that the activity of PcsB is regulated by the transmembrane FtsEX complex. In this work the muralytic activity of PcsB is demonstrated for the first time. Furthermore, we report the crystal structure of full-length PcsB showing an unprecedented dimeric structure in which the unique V-shaped coiled-coil domain of each monomer acts as a molecular tweezers locking down the catalytic domain of its dimeric partner in an inactive configuration. This finding strongly suggests that the release of the catalytic domains requires an ATP-driven conformational change in the FtsEX complex, which is most likely conveyed towards the catalytic domains through a set of coordinated movements of the α-helices forming the coiled-coil domain of PcsB.


Sergio G. Bartual, Daniel Straume, Gro Anita Stamsås, Inés G. Muñoz, Carlos Alfonso, Martín Martínez-Ripoll, Leiv Sigve Håvarstein* & Juan A. Hermoso *

Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniae

Nature Communications (2014). DOI: 10.1038/ncomms4842




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 (


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.
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

16th May of 2013