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Structural Biology Laboratory

logo                           Structural Biology Laboratory

The visualization of biological molecules at molecular and atomic detail  acilitates the rationalization of the chemical mechanisms underlying the biochemical phenomena in which they are involved. We have been using crystallographic X-rays diffraction analysis to study a variety of biological macromolecules. This technique has been highly successful in the 3D structural determination of biological macro-molecules. It requires a preliminary crystallization of the molecule under study, often in presence of reaction substrates or products analogues. Crystals diffraction data may be measured using in-house X-rays equipment, like those at the Macromolecular Crystallography Unit in ITQB, but their quality is greatly improved when also measured at synchrotron radiation facilities to which this Unit has routine access. The structural features of the obtained molecules may then be related with their biochemical properties. Comparisons may also be performed with other structures already available in data banks, like  the PDB, which  provide further clues on their structure-function relationships.  




Carlos Frazão
Investigador Principal

Phone (+351) 214469666/156


2008 to date       Group Leader, ITQB, Oeiras, Portugal
1990-2008          Researcher, ITQB, Oeiras, Portugal
1988-1990          PostDoc at Birkbeck College, University of London, UK
1984-1988          PhD Chemistry, TU Munich, Germany
1984                    Assistant Prof. Chemical Engineering, IST-UTL. Lisbon, Portugal
1979-1981          Pharmaceutical technician, Fidelis SARL, Oeiras, Portugal


Areas of research: I have been working on crystallographic studies of macromolecular biomolecules involved in:
1- protease activity
1.1.- aspartic proteases involved in blood pressure control, or in plant development and used in artesanal cheese manufacture
1.2. - cystein proteases
2 - bone formation/control (osteocalcins)
3 - electron transfer processes
3.1. - mono- and multi-heme cytochromes
3.2. - di-iron oxygen or nitric oxide oxido-reductases
3.3. - non-heme mono-iron sulfur oxidase reductases
3.4. - ferredoxins
3.4.1. - high potential iron proteins
3.4.2. - [3Fe-4S]1+/0 [4Fe-4S]2+/1+ Zn2+ ferredoxin
3.5. - hybrid cluster iron-sulfur protein
3.7. - Rieske protein
4. - ribonuclease II
5. - poly-saccharide synthesys
5.1. - UDP-glucose dehydrogenases
5.2. - glucose-1-phosphate uridylyltransferase
6. - amidase
7. - nitroreductase

Hints on ongoing research projects on  BceC, amidase or SOR are given at pages indicated above (top left).

At the moment I m also working with projects involving a new Rieske protein, a Yeast transcription factor,  two beta-myrcene catabolic enzymes and a phosphomannose isomerase.



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