Assessing the utility of coevolution-based residue-residue contact predictions in a sequence- and structure-rich era.
about
Sequence co-evolution gives 3D contacts and structures of protein complexesSequence co-evolutionary information is a natural partner to minimally-frustrated models of biomolecular dynamicsInferring Pairwise Interactions from Biological Data Using Maximum-Entropy Probability ModelsAn Integrated Framework Advancing Membrane Protein Modeling and DesignA structural model of the active ribosome-bound membrane protein insertase YidCLarge-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 ChaperonesEvolution-Based Functional Decomposition of ProteinsStructural and Functional Characterization of the Bacterial Type III Secretion Export ApparatusComparison of Algorithms for Prediction of Protein Structural Features from Evolutionary DataStructure and Sequence Analyses of Clustered Protocadherins Reveal Antiparallel Interactions that Mediate Homophilic SpecificityAntiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4Protein structure determination by combining sparse NMR data with evolutionary couplingsAmino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptorsAll-atom 3D structure prediction of transmembrane β-barrel proteins from sequencesPconsFold: improved contact predictions improve protein modelsFast and accurate multivariate Gaussian modeling of protein families: predicting residue contacts and protein-interaction partnersAccurate De Novo Prediction of Protein Contact Map by Ultra-Deep Learning ModelThe observation of evolutionary interaction pattern pairs in membrane proteins.Covariation Is a Poor Measure of Molecular Coevolution.Determining protein structures by combining semireliable data with atomistic physical models by Bayesian inferenceAccurate contact predictions using covariation techniques and machine learning.Protein contact prediction by integrating joint evolutionary coupling analysis and supervised learning.Large-scale determination of previously unsolved protein structures using evolutionary informationIntegration of QUARK and I-TASSER for Ab Initio Protein Structure Prediction in CASP11.Serum Albumin Domain Structures in Human Blood Serum by Mass Spectrometry and Computational BiologySome of the most interesting CASP11 targets through the eyes of their authorsImproved de novo structure prediction in CASP11 by incorporating coevolution information into Rosetta.Combining Evolutionary Information and an Iterative Sampling Strategy for Accurate Protein Structure Prediction.Residue proximity information and protein model discrimination using saturation-suppressor mutagenesisBlind testing of cross-linking/mass spectrometry hybrid methods in CASP11.CoeViz: a web-based tool for coevolution analysis of protein residues.Protein Residue Contacts and Prediction MethodsCritical assessment of methods of protein structure prediction: Progress and new directions in round XI.Theoretical Insights into the Biophysics of Protein Bi-stability and Evolutionary Switches.Detection and sequence/structure mapping of biophysical constraints to protein variation in saturated mutational libraries and protein sequence alignments with a dedicated serverAn algorithm to parse segment packing in predicted protein contact mapsResidue contacts predicted by evolutionary covariance extend the application of ab initio molecular replacement to larger and more challenging protein folds.Recent advances in sequence-based protein structure prediction.Simultaneous identification of specifically interacting paralogs and interprotein contacts by direct coupling analysis.Simultaneous Optimization of Biomolecular Energy Functions on Features from Small Molecules and Macromolecules.
P2860
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P2860
Assessing the utility of coevolution-based residue-residue contact predictions in a sequence- and structure-rich era.
description
2013 nî lūn-bûn
@nan
2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Assessing the utility of coevo ...... uence- and structure-rich era.
@ast
Assessing the utility of coevo ...... uence- and structure-rich era.
@en
type
label
Assessing the utility of coevo ...... uence- and structure-rich era.
@ast
Assessing the utility of coevo ...... uence- and structure-rich era.
@en
prefLabel
Assessing the utility of coevo ...... uence- and structure-rich era.
@ast
Assessing the utility of coevo ...... uence- and structure-rich era.
@en
P2860
P356
P1476
Assessing the utility of coevo ...... uence- and structure-rich era.
@en
P2093
Hetunandan Kamisetty
P2860
P304
15674-15679
P356
10.1073/PNAS.1314045110
P407
P577
2013-09-05T00:00:00Z