Researchers with the joint program between IRB Barcelona –located at the Parc Científic de Barcelona– and the Barcelona Supercomputing Center (BSC) have devised a new strategy to study the shape of proteins. This study has been led by Modesto Orozco, head of the Molecular Modeling and Bioinformatics Group, and Xavier Salvatella, head of the Molecular Biophysics Group, both ICREA scientists at IRB Barcelona. The results are available from today in the electronic version of the Proceedings of the National Academy of Sciences (PNAS).

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The study has several scientific implications, which can be summarized in the following three points. First of all, the researchers have described the chemical mechanisms by which compounds such as urea unfold proteins. “This was a debate that started in the 60s, and with this work it can now be considered closed”, explains Orozco.

Furthermore, they have established a new strategy that will allow them to decipher the conformation of the Intrinsically Disordered Proteins (IDP). IDPs are a group of proteins without a rigid structure that comprise a large part of the proteome; however, little is known about them. “Our results will contribute to research into diseases that involve IDPs, such as cancer, Parkinson’s or Alzheimer”, asserts Salvatella. Finally, the scientists have identified the first steps in protein folding, another topic that is widely contended.

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