RosettaEPR: an integrated tool for protein structure determination from sparse EPR data. - Wikidata - wikimedia - TriplyDB

RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

http://www.wikidata.org/entity/Q30395519

about

Use of electron paramagnetic resonance to solve biochemical problems Computational modeling of membrane proteins Sparse labeling of proteins: structural characterization from long range constraints BCL::Fold--de novo prediction of complex and large protein topologies by assembly of secondary structure elements Constraint methods that accelerate free-energy simulations of biomolecules Relative Orientation of POTRA Domains from Cyanobacterial Omp85 Studied by Pulsed EPR Spectroscopy.Assessment of CASP10 contact-assisted predictions.One contact for every twelve residues allows robust and accurate topology-level protein structure modeling Iterative Molecular Dynamics-Rosetta Protein Structure Refinement Protocol to Improve Model Quality.BCL::Fold--protein topology determination from limited NMR restraints.BCL::MP-fold: Membrane protein structure prediction guided by EPR restraints Improved cryoEM-Guided Iterative Molecular Dynamics--Rosetta Protein Structure Refinement Protocol for High Precision Protein Structure Prediction.Protein structure prediction guided by crosslinking restraints--A systematic evaluation of the impact of the crosslinking spacer length Determining protein structures by combining semireliable data with atomistic physical models by Bayesian inference Navigating Membrane Protein Structure, Dynamics, and Energy Landscapes Using Spin Labeling and EPR Spectroscopy.Blind testing of cross-linking/mass spectrometry hybrid methods in CASP11.Pushing the size limit of de novo structure ensemble prediction guided by sparse SDSL-EPR restraints to 200 residues: The monomeric and homodimeric forms of BAX Computational methods in drug discovery.Membrane protein structure determination using paramagnetic tags.Toward the fourth dimension of membrane protein structure: insight into dynamics from spin-labeling EPR spectroscopy EM-fold: de novo atomic-detail protein structure determination from medium-resolution density maps.MtsslWizard: In Silico Spin-Labeling and Generation of Distance Distributions in PyMOL.Accurate high-throughput structure mapping and prediction with transition metal ion FRET Structural refinement from restrained-ensemble simulations based on EPR/DEER data: application to T4 lysozyme.Monomeric and dimeric conformation of the vinculin tail five-helix bundle in solution studied by EPR spectroscopy.Alternative computational protocols for supercharging protein surfaces for reversible unfolding and retention of stability RosettaEPR: rotamer library for spin label structure and dynamics.Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit.Accelerating molecular simulations of proteins using Bayesian inference on weak information.Conformation of receptor-bound visual arrestin.Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN(-) binding defined by EPR-based hybrid method.Protonation-dependent conformational dynamics of the multidrug transporter EmrE.Determining the Secondary Structure of Membrane Proteins and Peptides Via Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy Restrained-ensemble molecular dynamics simulations based on distance histograms from double electron-electron resonance spectroscopy.Protocols for Molecular Modeling with Rosetta3 and RosettaScripts TagDock: an efficient rigid body docking algorithm for oligomeric protein complex model construction and experiment planning.Energetic analysis of the rhodopsin-G-protein complex links the α5 helix to GDP release.Modeling helical proteins using residual dipolar couplings, sparse long-range distance constraints and a simple residue-based force field.Small-molecule ligand docking into comparative models with Rosetta.Structure and Dynamics of Type III Secretion Effector Protein ExoU As determined by SDSL-EPR Spectroscopy in Conjunction with De Novo Protein Folding

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RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

http://www.wikidata.org/entity/Q30395519

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

@ast

RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

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type

label

RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

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RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

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prefLabel

RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

@ast

RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

@en

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J.JSB.2010.10.013

P1433

Journal of Structural Biology

P1476

RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.

@en

P2093

Hassane S McHaourab

http://www.w3.org/2001/XMLSchema#string

Nathan Alexander

http://www.w3.org/2001/XMLSchema#string

Stephanie J Hirst

http://www.w3.org/2001/XMLSchema#string

P2860

NMR structure determination for larger proteins using backbone-only data

Consistent blind protein structure generation from NMR chemical shift data

Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating

Structure of the KcsA channel intracellular gate in the open state

Structural origin of weakly ordered nitroxide motion in spin-labeled proteins

Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution

Protein secondary structure prediction based on position-specific scoring matrices

Rotamer libraries in the 21st century

Rosetta in CASP4: progress in ab initio protein structure prediction

Structure prediction for CASP7 targets using extensive all-atom refinement with Rosetta@home

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506-514

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10.1016/J.JSB.2010.10.013

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3

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173

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47620793

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21029778

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protein structure

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3040274

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