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Study and modeling of processes involving proteins
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We have performed studies of protein folding processes, protein conformational changes and protein interactions with molecules of pharmacological, biological or environmental interest. Process monitoring is carried out using spectroscopic techniques, such as circular dichroism, fluorescence, molecular absorption, IR or mass spectrometry. The recorded data are analyzed with multivariate resolution techniques, developed in our research group.


The biological interest of these studies is complemented by the methodological approach used to get the process description. Given the high complexity of biological processes, the strategies used in the experimental monitoring and interpretation of the information can be extended to the analysis of processes taking place in environmental or industrial scenarios.

 

Most relevant publications

1. Detection and resolution of intermediate species in protein unfolfing and folding processes using fluorescence and circular dichroism spectroscopies and multivariate curve resolution. Navea, S.; de Juan, A.; Tauler, R. Analytical Chemistry, 64 (2002) 6031 -6039.
2. Modelling temperature-dependent protein structural transitions by combined NIR and MIR spectroscopies and multivariate curve resolution. S.Navea, A. de Juan and R.Tauler. Analytical Chemistry, 2003, 75, 5592-5601.
3. Application of multivariate curve resolution to the temperature-induced unfolding of alpha-chymotrypsin. Borges, A.; Tauler, R.; de Juan, A. Analytica Chimica Acta, 544 (2005) 159-166.
4. Chemometrics tools for classification and elucidation of protein secondary structure from infrared and circular dichroism spectroscopic measurements. Susana Navea, Romà Tauler, Anna de Juan. Proteins-Structure Function and Genetics, 63 (2006) 527-541.
5. Monitoring and modelling of protein processes using Mass Spectrometry, Circular Dichroism and multivariate resolution methods. Navea, S.; Tauler, R.; de Juan, A. Analytical Chemistry 78 (2006) 4768-4778.
6. pH- and time-dependent hemoglobin transitions: a case study for process modelling. Muñoz, G.; de Juan, A. Analytica Chimica Acta, 595 (2007) 198-208.

 

 
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Selected presentation

 

Chemometric tools for multitechnique and multiexperiment protein process analysis

 

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Última actualització o validació: 28.10.2007
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