CERM

  

Welcome to the
Magnetic Resonance Center (CERM)

CERM is a center for research, knowledge transfer, and higher education of the University of Florence, located at the Polo Scientifico (Scientific Campus) in Sesto Fiorentino.

The Center is a research infrastructure for NMR in the Life Sciences supported by the European Community.

Research Activity

  

Goals of our Research in Structural Biology

1) Encourage activities and competencies as a world-class infrastructure in NMR that are second to none
2) Use of a bioinformatics approach that allows for the prioritization of proteins of interest
3) Production of proteins using approaches that lend themselves to high-throughput research
4) Structural determination and study of protein-protein/protein-ligand interactions using NMR, and when appropriate, X-ray technologies
5) Drug design and development at all stages, from planning to chemical synthesis to control of target interaction

To learn more about the research activities of CERM, please go here or follow the links above.

Access to Unique Instrumentation

  

Access to Instrumentation Provided by CIRMMP

The collection of instrumentation at CERM is among the most advanced in the world.  The Consorzio Interuniversitario Risonanze Magnetiche di Metalloproteine Paramagnetiche (CIRMMP) provides access to equipment at a national and European level.

Instruments include magnets from 400 MHz to 900 MHz, many equipped with unique probes for disparate experimental needs.  Also present are relaxometers and an array of tools for research in structural biology.

To learn more about our instrumentation and access, please click here.

Academic Opportunities

  

International Doctorate in Structural Biology and Marie Curie Fellowships

CERM is the reference institution for the International Doctorate in Structural Biology, organized in collaboration with the Universities of Frankfurt and Utrecht.

CERM is active as a Marie Curie training site to host European Ph.D. students, and has organized many international conferences

The CERM staff is also involved with students during their undergraduate years, and organizes countless seminars and courses for the training of internal personnel.

CERM in the Headlines:

HRH the Princess of Thailand Chulabhorn Mahidol visits CERM

HRH Chulabhorn Mahidol, Princess of Thailand and President of the Chulabhorn Research Institute, visited CERM on August 24th.  She is pictured here with the Director of CERM, Iv...
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Ivano Bertini featured in Nature Chemical Biology

Building on his contributions to NMR methodologies for studying metalloproteins, Bertini has been instrumental in bringing together inorganic chemists and biologists interested in metals in biology. H...
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Amyotrophic Lateral Sclerosis - Protein Cause Discovered

(September 18, 2007)  The causes and the molecular mechanism of the malfunctioning of this protein have been characterized by researchers from the Florence-based company FiorGen.  Supe...
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Archives

News and publicity archives dating back to 2000 ...
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CERM research published in Nature
Affinity gradients drive copper to cellular destinations
A group of CERM researchers has determined, through a unified electrospray ionization mass spectrometry (ESI-MS)-based strategy, in an environment that mimics the cellular redox milieu, the apparent Cu(I)-binding affinities for a representative set of intracellular copper proteins involved in enzymatic redox catalysis, in copper trafficking to and within various cellular compartments, and in copper storage. The resulting thermodynamic data show that copper is drawn to the enzymes that require it by passing from one copper protein site to another, exploiting gradients of increasing copper-binding affinity. 

Please click here for the link to the article.

Hot off the Press:

Ultrafast MAS solid-state NMR permits extensive (13)C and (1H) detection in paramagnetic metalloproteins

We show here that by combining tailored approaches based on ultrafast (60 kHz) MAS on the Co(II)-replaced catalytic domain of matrix metalloproteinase 12 (CoMMP-12) we can observe and assign, in a highly paramagnetic protein in the solid state, (13)C and even (1)H resonances from the residues coordinating the metal center. In addition, by exploiting the enhanced relaxation caused by the paramagnetic center, and the low power irradiation enabled by the fast MAS, this can be achieved in remarkably short times and at very high field (21.2 T), with only less than 1 mg of sample. Furthermore, using the known crystal structure of the compound, we are able to distinguish and measure pseudocontact (PCS) contributions to the shifts up to the coordinating ligands and to unveil structural information. Please click here for the link to the article


New drug design proceeds
thanks to the Monte dei Paschi di Siena Foundation


The research project "Identifying ligands and binding sites on pharmacological target proteins for future new drug design" financed by the Monte dei Paschi di Siena Foundation focuses on the development of small-molecule modulators of protein-protein interactions, using NMR spectroscopy to monitor small-molecule binding to the two proteins of pharmaceutical relevance, S100B and Bcl-xL. NMR-based identification of the hot spots on the protein surfaces relies on the use of Garrett plots that provide chemical shift mapping of the protein residues involved in the interaction. This structural information, in conjunction with estimates of the Kd and ligand efficiency values, will provide the basis for further ligand optimization. The project is expected to have significant impact on the discovery of novel therapeutics.

This study has recently been accepted for publication in Chembiochem: "Fragmenting the S100B-p53 interaction - Combined virtual/biophysical screening approaches to identify ligands", by Alessandro Padova


High-resolution solid-state NMR structure of a 17.6 kDa protein solved

As recently published in the Journal of the American Chemical Society, pseudocontact shifts arising from paramagnetic metal ions in a microcrystalline protein sample have been used to obtain unambiguous signal assignments in solid-state NMR spectra, enabling distance extraction for protein structure calculation. The resulting structure is high-resolution and in good agreement with the X-ray structure. This strategy may be generalized for non-metalloproteins through the use of paramagnetic tags, and represents a significant step ahead in protein structure determination using solid-state NMR. Please click here for the link to the article.


Partner Institutions

     
    
     



                                      
                                                                   
 

Upcoming Meetings

Worldwide Magnetic Resonance Conference 2010
Florence, July 4-9, 2010

Click here for more information on meetings past and present.

Upcoming Seminars

Research Seminar Series
Seminars are held every week from 1:30 - 2:00 pm
in the CERM Conference Room

August 26
Anna Pavelkova

2010 RSS Calendar


Click here for more information on seminars past and present.