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Protein Residue Contacts and Prediction MethodsResidue contacts predicted by evolutionary covariance extend the application of ab initio molecular replacement to larger and more challenging protein folds.Potts Hamiltonian models of protein co-variation, free energy landscapes, and evolutionary fitness.Correlated mutations select misfolded from properly folded proteins.Membrane protein contact and structure prediction using co-evolution in conjunction with machine learning.New Techniques for Ancient Proteins: Direct Coupling Analysis Applied on Proteins Involved in Iron Sulfur Cluster BiogenesisInter-Protein Sequence Co-Evolution Predicts Known Physical Interactions in Bacterial Ribosomes and the Trp OperonACE: adaptive cluster expansion for maximum entropy graphical model inference.Optimization of sequence alignments according to the number of sequences vs. number of sites trade-off.Maximum-Entropy Models of Sequenced Immune Repertoires Predict Antigen-Antibody Affinity.Inferring Contacting Residues within and between Proteins: What Do the Probabilities Mean?The Maximum Entropy Fallacy Redux?Interacting networks of resistance, virulence and core machinery genes identified by genome-wide epistasis analysis.An overview of comparative modelling and resources dedicated to large-scale modelling of genome sequences.Comparing co-evolution methods and their application to template-free protein structure prediction.Direct coevolutionary couplings reflect biophysical residue interactions in proteins.Identifying relevant positions in proteins by Critical Variable Selection.New encouraging developments in contact prediction: Assessment of the CASP11 results.A Biologically-validated HCV E1E2 Heterodimer Structural Model.RRCRank: a fusion method using rank strategy for residue-residue contact predictionObservation selection bias in contact prediction and its implications for structural bioinformaticsAssessment of contact predictions in CASP12: co-evolution and deep learning coming of age.Identifying Functionally Informative Evolutionary Sequence Profiles.Forecasting residue-residue contact prediction accuracy.Patterns of coevolving amino acids unveil structural and dynamical domains.Biomolecular coevolution and its applications: Going from structure prediction toward signaling, epistasis, and function.Three-body interactions improve contact prediction within direct-coupling analysis.MISTIC2: comprehensive server to study coevolution in protein families.
P2860
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P2860
description
2014 nî lūn-bûn
@nan
2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年学术文章
@wuu
2014年学术文章
@zh-cn
2014年学术文章
@zh-hans
2014年学术文章
@zh-my
2014年学术文章
@zh-sg
2014年學術文章
@yue
name
Improving contact prediction along three dimensions.
@ast
Improving contact prediction along three dimensions.
@en
Improving contact prediction along three dimensions.
@nl
type
label
Improving contact prediction along three dimensions.
@ast
Improving contact prediction along three dimensions.
@en
Improving contact prediction along three dimensions.
@nl
prefLabel
Improving contact prediction along three dimensions.
@ast
Improving contact prediction along three dimensions.
@en
Improving contact prediction along three dimensions.
@nl
P2860
P1476
Improving contact prediction along three dimensions.
@en
P2093
Christoph Feinauer
Erik Aurell
P2860
P304
P356
10.1371/JOURNAL.PCBI.1003847
P577
2014-10-09T00:00:00Z