María Inés Freiberger

Proteome-wide prediction of the Functional Impact of Missense Variants with ProteoCast

ProteoCast predicts the functional impact of missense variants using evolutionary information, achieving high accuracy across the Drosophila proteome.

ProteoCast: a web server to predict, validate, and interpret missense variant effects

ProteoCast predicts and interprets missense variant effects using evolutionary and structural analysis, achieving high accuracy in pathogenicity prediction and identifying functional motifs in disordered regions.

Predicting the dynamic interaction of intrinsically disordered proteins

This paper introduces GSALIDP, a model that predicts dynamic interactions of intrinsically disordered proteins using graph and sequence-based methods, achieving performance comparable to or better than existing models.

Frustraevo: A Web Server To Localize And Quantify The Conservation Of Local Energetic Frustration In Protein Families

FrustraEvo calculates and quantifies the conservation of local energetic frustration in protein families to identify evolutionary stability and functional constraints.

The Evolution of Local Energetic Frustration in Protein Families

The paper analyzes local energetic frustration in protein families to uncover stability and function constraints, demonstrating its application to SARS-CoV-2 and poorly characterized proteins.

FrustraPocket: A protein-ligand binding site predictor using energetic local frustration

FrustraPocket identifies protein-ligand binding sites from unbound protein structures by detecting regions of local energetic frustration.

FrustratometeR: an R-package to compute Local frustration in protein structures, point mutants and MD simulations

FrustratometeR computes local energetic frustration in protein structures, point mutants, and MD simulations for structural analysis.

Frustration in protein complexes leads to interaction versatility

The paper shows that disordered proteins in fuzzy complexes retain residual frustration, leading to interaction versatility with different partners.

Large Ankyrin repeat proteins are formed with similar and energetically favorable units

The paper analyzes a large dataset of Ankyrin-containing proteins to characterize the structure, abundance, and energetics of their repetitive regions, finding that longer arrays have more similar repeats and favorable folding energy.