Author

P. F. Faisca

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

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Research Focus:protein folding & dynamics· 4 Assay:protein structure· 3 Approach:statistical model· 3 Approach:mechanistic / dynamical model· 1 Approach:simulation· 1

Frequent Co-Authors

A. Nunes· 1 shared F. E. P. Rodrigues· 1 shared J. Especial· 1 shared J. Morand· 1 shared J. N. Especial· 1 shared J. N. M. Vitorino· 1 shared M. Machuqueiro· 1 shared N. F. B. Oliveira· 1 shared

Activity by Year

2021-2023 · peak 3/yr

Co-Author Collaboration Network

9 top collaborators · 11 mutual co-author links

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1 shared paperBiophysics

A. Nunes

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4 papers

Recent·Most cited

Effects of sequence-dependent non-native interactions in equilibrium and kinetic folding properties of knotted proteins

P. F. Faisca, J. N. Especial

This study uses simulations to show non-native interactions enhance knotted protein folding efficiency but are not required for efficient folding.

bioRxiv · Jun 6, 2023 · PreprintBiophysics

Predicting stable binding modes from simulated dimers of the D76N mutant of β2-microglobulin

N. F. B. Oliveira, F. E. P. Rodrigues, J. N. M. Vitorino, R. J. S. Loureiro, P. F. Faisca, M. Machuqueiro

This paper uses molecular dynamics simulations and MM-PBSA calculations to analyze dimer stability of the D76N β2m mutant, finding hydrophobic interactions and terminal regions drive interface stability.

bioRxiv · Jul 14, 2021Biophysics

A specific set of heterogeneous native interactions yields efficient knotting in protein folding

J. Especial, P. F. Faisca

This study shows that specific heterogeneous native interactions can efficiently knot proteins without requiring non-native interactions, using Monte Carlo simulations of lattice models.

bioRxiv · May 19, 2021 · PreprintBiophysics

The folding space of protein β2-microglobulin is modulated by a single disulfide bond

J. Morand, A. Nunes, P. F. Faisca

This study investigates how a single disulfide bond modulates the folding behavior of β2-microglobulin using molecular dynamics simulations, revealing its impact on intermediate states and aggregation potential.

bioRxiv · May 19, 2021Biophysics