Patricia Faísca

Contactos

Departamento de Física

Sala/Gabinete C8-P4
Ext. Principal 28607
Telefone Direto
Email pffaisca@ciencias.ulisboa.pt
Página Pessoal

Carreira Docente Universitário
Categoria Professor Auxiliar

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Currículo Resumido

Patrícia F.N. Faísca is Assistant Professor of Physics at the Physics Department of the Faculty of Sciences (DF-FCUL), University of Lisbon, and principal investigator at BioISI – Biosystems and Integrative Sciences Institute. She received her PhD (Physics) in 2002 at the University of Warwick (UK), as part of the Gulbenkian PhD Program in Biology and Medicine. She has a broad interdisciplinary education covering Physics, Biology and Mathematics. Her research on computational biophysics is based on the use of molecular simulations, especially of coarse-grained models. Her current research interests focus on the folding of knotted proteins, and on protein misfolding and aggregation in a disease-related context.


Interesses Científicos

Física interdisciplinar, física biológica (teoria e simulação de 'folding' e agregação de proteínas), física computacional, física estatística


Scientific Interests

Interdisciplinary physics, biological physics (theory and simulations of protein folding and aggregation), computational physics, statistical physics


Publicações selecionadas
  • Heinrich Krobath, Antonio Rey and Patricia FN Faísca “How determinant is N-terminal to C-terminal coupling for protein folding?” Physical Chemistry and Chemical Physics 17, 3512-3524 (2015)
  • MA Soler, A Rey, PFN Faísca Steric confinement and enhanced local flexibility assist knotting in simple models of protein folding Physical Chemistry Chemical Physics 18:26391-26403 (2016)
  • SG Estácio, H Krobath, D Vila-Viçosa, M Machuqueiro, EI Shakhnovich, PFN Faísca “A simulated intermediate state for folding and aggregation provides new insights into 2-microglobulin amyloidogenic behavior” PLoS Computational Biology 10: e1003606 (2014)
  • PFN Faísca Knotted Proteins: A tangled tale of structural biology (Invited Review) Computational and Structural Biotechnology Journal 13:459-468 (2015)
  • J Especial, A Nunes, A Rey, PFN Faísca Hydrophobic confinement modulates thermal stability and assists knotting in the folding of tangled proteins Physical Chemistry Chemical Physics 21:11764-11775 (2019)

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