Eduardo Oliveira Calçada


Eduardo Calçada graduated in Biochemistry at the Universidade da Beira Interior (UBI) where he wrote his thesis concerning new methods for purifications of β-amyloid antibodies for therapeutic use. After his graduation did a pos-graduation in Legal Medicine Sciences at Instituto de Ciências Biomédicas Abel Salazar at Universidade do Porto (ICBAS/UP). He continued his studies with a Master in Biochemistry, where he developed his knowledge on electron transfer biochemistry of cytochromes at Instituto de Tecnologia Química e Biológica (ITQB) under the supervision of Doctor Ricardo O. Louro. After his graduation joined the MIT-Portugal project under bio-energy production, where he developed his skills in proteomics. He was also a fellow at REQUIMTE under the same project. Eduardo developed an outstanding interest in protein function research based on his background in biochemistry and molecular biology. Within the IDPbyNMR project he has been appointed by CERM group. On January 2014 he finished the International Doctorate program in Mechanistic and Structural Systems Biology, presenting his PhD thesis "Intrinsically disordered proteins - from sample preparation to molecular basis of function" which was classified as excelent.


Eduardo Oliveira Calçada
Project Topic
Flavours of Disorder: all the way to in-cell
Brief Project Description
Many functional proteins are devoid of stable secondary and tertiary structure. They are known as intrinsically disordered proteins (IDPs) and play important functions including molecular recognition, signaling, and regulation with implication in several human diseases like Alzheimer, Parkinson, cancer and many viral infections. The lack of dynamic ensembles of conformations under physiological conditions makes their analysis difficult to achieve. NMR has been shown to be an useful tool to analyze IDPs. In-cell NMR experiments enables the ability to observe IDPs in an environment similar to the natural one. Understanding IDPs allows to better knowing how these proteins are involved in molecular pathways of human disorders.
Project Home
Supervisor Roberta Pierattelli, Isabella C. Felli
Starting Date 04/04/2011

Calçada, E.O., Felli, I.C., Hošek, T., and Pierattelli, R. 
The heterogeneous structural behavior of E7 from HPV16 revealed by NMR spectroscopy. 
ChemBioChem 14, 1876–1882. (2013)



Intensive Training Course
Intellectual Properties Rights and Finances,
September 4-6, 2013 - Zurich, Switzerland

SAXS and computational techniques to study intrinsically disordered proteins
March 2013 - Hamburg, Germany

NMR methods for the study of structural order and disorder in proteins
September 2012 - Les Houches, France

Intensive Training Module – Marie Curie Training Network
Protein Structure Analysis using NMR Chemical Shifts
May 2012 - Cambridge, United Kingdom

Complementary Skills Training – Marie Curie Training Network
Self Marketing, Project Management, Benchmarks and Competition in Research
February 2012 - St. Moritz, Switzerland

Intensive Training Module – Marie Curie Training Network
Structural and Unstructural Biology of Viral Proteins
January 2012  - Florence, Italy

Intensive Training Course 2011 – Marie Curie Training Network
Bioinformatics and Structural biology of IDPs
October 2011 - Budapest, Hungary

Bio-NMR satellite meeting of the FEBS annual congress 2011
NMR in Biology
June 2011 - Lingotto Conference Center, Turin, Italy



Scientific Posters:


Human Papilloma Virus intrinsically disordered protein E7 characterization by NMR spectroscopy
FEBS & IUBMB 2012 congress, Seville, Spain
September, 2012