Direct-coupling analysis is a statistical learning method for protein contact prediction based on sequence information alone. The maximum entropy principle leads to an effective inverse Potts model. Predictions on contacts are based on fitted local fields and couplings from an empirical multiple sequence alignment. Typically, the l_{2} norm of the resulting two-body couplings is used for contact prediction. However, this procedure discards important information. In this paper we show that the usage of the full fields and coupling information improves prediction accuracy
Correlation patterns in multiple sequence alignments of homologous proteins can be exploited to infe...
Compensatory mutations between protein residues in physical contact can manifest themselves as stati...
<div><p>Correlation patterns in multiple sequence alignments of homologous proteins can be exploited...
International audienceSpatially proximate amino acids in a protein tend to coevolve. A protein's thr...
Abstract Background Direct-coupling analysis (DCA) is a method for protein contact prediction from s...
Protein Direct Coupling Analysis (DCA), which predicts residue-residue contacts based on covarying p...
International audienceCoevolution of residues in contact imposes strong statistical constraints on t...
International audienceCoevolution of residues in contact imposes strong statistical constraints on t...
Co-evolution between pairs of residues in a multiple sequence alignment (MSA) of homologous proteins...
Protein Direct Coupling Analysis (DCA), which predicts residue-residue contacts based on covarying p...
BACKGROUND Direct-coupling analysis (DCA) is a method for protein contact prediction from sequenc...
<div><p>Co-evolution between pairs of residues in a multiple sequence alignment (MSA) of homologous ...
The recent application of models from inverse statistical mechanics to protein sequence data in has ...
Correlation patterns in multiple sequence alignments of homologous proteins can be exploited to infe...
Amino acids that are in close contact in a protein structure tend to co-evolve, which gives rise to ...
Correlation patterns in multiple sequence alignments of homologous proteins can be exploited to infe...
Compensatory mutations between protein residues in physical contact can manifest themselves as stati...
<div><p>Correlation patterns in multiple sequence alignments of homologous proteins can be exploited...
International audienceSpatially proximate amino acids in a protein tend to coevolve. A protein's thr...
Abstract Background Direct-coupling analysis (DCA) is a method for protein contact prediction from s...
Protein Direct Coupling Analysis (DCA), which predicts residue-residue contacts based on covarying p...
International audienceCoevolution of residues in contact imposes strong statistical constraints on t...
International audienceCoevolution of residues in contact imposes strong statistical constraints on t...
Co-evolution between pairs of residues in a multiple sequence alignment (MSA) of homologous proteins...
Protein Direct Coupling Analysis (DCA), which predicts residue-residue contacts based on covarying p...
BACKGROUND Direct-coupling analysis (DCA) is a method for protein contact prediction from sequenc...
<div><p>Co-evolution between pairs of residues in a multiple sequence alignment (MSA) of homologous ...
The recent application of models from inverse statistical mechanics to protein sequence data in has ...
Correlation patterns in multiple sequence alignments of homologous proteins can be exploited to infe...
Amino acids that are in close contact in a protein structure tend to co-evolve, which gives rise to ...
Correlation patterns in multiple sequence alignments of homologous proteins can be exploited to infe...
Compensatory mutations between protein residues in physical contact can manifest themselves as stati...
<div><p>Correlation patterns in multiple sequence alignments of homologous proteins can be exploited...