Improving NMR protein structure quality by Rosetta refinement: A molecular replacement study - Test2 - elhamkhani - TriplyDB

Improving NMR protein structure quality by Rosetta refinement: A molecular replacement study

Improving NMR protein structure quality by Rosetta refinement: A molecular replacement study

http://www.wikidata.org/entity/Q27652286

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Structural basis for cell surface patterning through NetrinG-NGL interactions Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples Quantum-mechanics-derived 13Calpha chemical shift server (CheShift) for protein structure validation Synergy of NMR, Computation, and X-Ray Crystallography for Structural Biology Solution Structure of 4′-Phosphopantetheine - GmACP3 from Geobacter metallireducens : A Specialized Acyl Carrier Protein with Atypical Structural Features and a Putative Role in Lipopolysaccharide Biosynthesis Structural analysis of a putative family 32 carbohydrate-binding module from theStreptococcus pneumoniaeenzyme EndoD Crystal structure of the intraflagellar transport complex 25/27 Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods PDBStat: a universal restraint converter and restraint analysis software package for protein NMR Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction Architecture and function of IFT complex proteins in ciliogenesis Computational modeling of laminin N-terminal domains using sparse distance constraints from disulfide bonds and chemical cross-linking MOTOR: model assisted software for NMR structure determination.Quality assessment of protein NMR structures.Protein NMR structures refined with Rosetta have higher accuracy relative to corresponding X-ray crystal structures Protein NMR structures refined without NOE data Residue-level global and local ensemble-ensemble comparisons of protein domains.Unique opportunities for NMR methods in structural genomics.Practically useful: what the Rosetta protein modeling suite can do for you Aromatic claw: A new fold with high aromatic content that evades structural prediction.Alternate states of proteins revealed by detailed energy landscape mapping High quality NMR structures: a new force field with implicit water and membrane solvation for Xplor-NIH.Advances in automated NMR protein structure determination.Resolution-by-proxy: a simple measure for assessing and comparing the overall quality of NMR protein structures.The quality and validation of structures from structural genomics.Trapping a salt-dependent unfolding intermediate of the marginally stable protein Yfh1.Accurate automated protein NMR structure determination using unassigned NOESY data.HA-tagging of putative flagellar proteins in Chlamydomonas reinhardtii identifies a novel protein of intraflagellar transport complex B.MolProbity for the masses-of data.phenix.mr_rosetta: molecular replacement and model rebuilding with Phenix and Rosetta.Improved crystallographic models through iterated local density-guided model deformation and reciprocal-space refinement.Assessing the chemical accuracy of protein structures via peptide acidity.Improved technologies now routinely provide protein NMR structures useful for molecular replacement.X-ray vs. NMR structures as templates for computational protein design.Collective variable approaches for single molecule flexible fitting and enhanced sampling.Structural studies of ciliary components.Residue-centric modeling and design of saccharide and glycoconjugate structures.Why proteins without an alpha-crystallin domain should not be included in the human small heat shock protein family HSPB.

P2860

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P2860

Improving NMR protein structure quality by Rosetta refinement: A molecular replacement study

http://www.wikidata.org/entity/Q27652286

description

2009 nî lūn-bûn

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2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2009 թվականի ապրիլին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Improving NMR protein structur ...... A molecular replacement study

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Improving NMR protein structur ...... A molecular replacement study

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Improving NMR protein structur ...... A molecular replacement study

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type

label

Improving NMR protein structur ...... A molecular replacement study

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Improving NMR protein structur ...... A molecular replacement study

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Improving NMR protein structur ...... A molecular replacement study

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Improving NMR protein structur ...... A molecular replacement study

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Improving NMR protein structur ...... A molecular replacement study

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Improving NMR protein structur ...... A molecular replacement study

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Improving NMR protein structur ...... A molecular replacement study

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Alexandre P Kuzin

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

John F Hunt

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

Li-Chung Ma

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

Michael A Kennedy

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

Rong Xiao

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

Srivatsan Raman

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

Theresa A Ramelot

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

Thomas B Acton

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

P2860

Design of a Novel Globular Protein Fold with Atomic-Level Accuracy

The Protein Data Bank

High-resolution structure prediction and the crystallographic phase problem

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex

Solution NMR structure of the barrier-to-autointegration factor-Emerin complex

Crystal structure of interleukin 8: symbiosis of NMR and crystallography

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147-67

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scholarly article

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10.1002/PROT.22229

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P433

1

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P478

75

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P50

Gaetano T. Montelione

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2009-04-01T00:00:00Z

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23281247

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18816799

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protein structure

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2878636

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