Search Results for author: Martin Weigt

Found 11 papers, 3 papers with code

Emergent time scales of epistasis in protein evolution

no code implementations14 Mar 2024 Leonardo Di Bari, Matteo Bisardi, Sabrina Cotogno, Martin Weigt, Francesco Zamponi

Our model uncovers a highly collective nature of epistasis, gradually changing the fitness effect of mutations in a diverging sequence context, rather than acting via strong interactions between individual mutations.

Towards Parsimonious Generative Modeling of RNA Families

1 code implementation19 Oct 2023 Francesco Calvanese, Camille N. Lambert, Philippe Nghe, Francesco Zamponi, Martin Weigt

Generative probabilistic models emerge as a new paradigm in data-driven, evolution-informed design of biomolecular sequences.

Combining phylogeny and coevolution improves the inference of interaction partners among paralogous proteins

no code implementations24 Aug 2022 Carlos A. Gandarilla-Perez, Sergio Pinilla, Anne-Florence Bitbol, Martin Weigt

We show that these two signals can be combined to improve the performance of the inference of interaction partners among paralogs.

Epistatic models predict mutable sites in SARS-CoV-2 proteins and epitopes

no code implementations19 Dec 2021 Juan Rodriguez-Rivas, Giancarlo Croce, Maureen Muscat, Martin Weigt

The emergence of new variants of SARS-CoV-2 is a major concern given their potential impact on the transmissibility and pathogenicity of the virus as well as the efficacy of therapeutic interventions.

adabmDCA: Adaptive Boltzmann machine learning for biological sequences

1 code implementation9 Sep 2021 Anna Paola Muntoni, Andrea Pagnani, Martin Weigt, Francesco Zamponi

Boltzmann machines are energy-based models that have been shown to provide an accurate statistical description of domains of evolutionary-related protein and RNA families.

BIG-bench Machine Learning

Modeling sequence-space exploration and emergence of epistatic signals in protein evolution

no code implementations4 Jun 2021 Matteo Bisardi, Juan Rodriguez-Rivas, Francesco Zamponi, Martin Weigt

During their evolution, proteins explore sequence space via an interplay between random mutations and phenotypic selection.

Efficient generative modeling of protein sequences using simple autoregressive models

no code implementations4 Mar 2021 Jeanne Trinquier, Guido Uguzzoni, Andrea Pagnani, Francesco Zamponi, Martin Weigt

Generative models emerge as promising candidates for novel sequence-data driven approaches to protein design, and for the extraction of structural and functional information about proteins deeply hidden in rapidly growing sequence databases.

Protein Design

Global multivariate model learning from hierarchically correlated data

no code implementations11 Feb 2021 Edwin Rodriguez Horta, Alejandro Lage, Martin Weigt, Pierre Barrat-Charlaix

The naive application of inverse statistical physics techniques therefore leads to systematic biases and an effective reduction of the sample size.

Disordered Systems and Neural Networks Statistical Mechanics Quantitative Methods

Sparse generative modeling via parameter-reduction of Boltzmann machines: application to protein-sequence families

no code implementations23 Nov 2020 Pierre Barrat-Charlaix, Anna Paola Muntoni, Kai Shimagaki, Martin Weigt, Francesco Zamponi

For example, pairwise Potts models (PM), which are instances of the BM class, provide accurate statistical models of families of evolutionarily related protein sequences.

Aligning biological sequences by exploiting residue conservation and coevolution

no code implementations18 May 2020 Anna Paola Muntoni, Andrea Pagnani, Martin Weigt, Francesco Zamponi

Here, we present DCAlign, an efficient alignment algorithm based on an approximate message-passing strategy, which is able to overcome the limitations of profile models, to include coevolution among positions in a general way, and to be therefore universally applicable to protein- and RNA-sequence alignment without the need of using complementary structural information.

Inverse Statistical Physics of Protein Sequences: A Key Issues Review

1 code implementation3 Mar 2017 Simona Cocco, Christoph Feinauer, Matteo Figliuzzi, Remi Monasson, Martin Weigt

In the course of evolution, proteins undergo important changes in their amino acid sequences, while their three-dimensional folded structure and their biological function remain remarkably conserved.

Cannot find the paper you are looking for? You can Submit a new open access paper.