SAGA: rapid automatic mainchain NMR assignment for large proteins.
about
The J-UNIO protocol for automated protein structure determination by NMR in solutionSolution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect.EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance dataA unified NMR strategy for high-throughput determination of backbone fold of small proteins.Facile backbone (1H, 15N, 13Ca, and 13C') assignment of 13C/15N-labeled proteins using orthogonal projection planes of HNN and HN(C)N experiments and its automation.RASP: rapid and robust backbone chemical shift assignments from protein structure.APSY-NMR for protein backbone assignment in high-throughput structural biology.Fast and accurate resonance assignment of small-to-large proteins by combining automated and manual approaches.Structure-Based Assignment of Ile, Leu, and Val Methyl Groups in the Active and Inactive Forms of the Mitogen-Activated Protein Kinase Extracellular Signal-Regulated Kinase 2Advances in automated NMR protein structure determination.AUTOBA: automation of backbone assignment from HN(C)N suite of experiments.Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme.Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α3DIV, that Sequesters Toxic Heavy MetalsNon-Uniform Sampling and J-UNIO Automation for Efficient Protein NMR Structure Determination.Chemical shift assignments of domain 4 from the phosphohexomutase from Pseudomonas aeruginosa suggest that freeing perturbs its coevolved domain interface.Detecting and accounting for multiple sources of positional variance in peak list registration analysis and spin system grouping.Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones.Enhanced biosynthetically directed fractional carbon-13 enrichment of proteins for backbone NMR assignments.Pseudo-4D triple resonance experiments to resolve HN overlap in the backbone assignment of unfolded proteins.The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.TSAR: a program for automatic resonance assignment using 2D cross-sections of high dimensionality, high-resolution spectra.Automated robust and accurate assignment of protein resonances for solid state NMR.Reduced dimensionality (3,2)D NMR experiments and their automated analysis: implications to high-throughput structural studies on proteins.RDC derived protein backbone resonance assignment using fragment assembly.
P2860
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P2860
SAGA: rapid automatic mainchain NMR assignment for large proteins.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年學術文章
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name
SAGA: rapid automatic mainchain NMR assignment for large proteins.
@en
SAGA: rapid automatic mainchain NMR assignment for large proteins.
@nl
type
label
SAGA: rapid automatic mainchain NMR assignment for large proteins.
@en
SAGA: rapid automatic mainchain NMR assignment for large proteins.
@nl
prefLabel
SAGA: rapid automatic mainchain NMR assignment for large proteins.
@en
SAGA: rapid automatic mainchain NMR assignment for large proteins.
@nl
P2093
P2860
P1476
SAGA: rapid automatic mainchain NMR assignment for large proteins.
@en
P2093
Aikaterini Rousaki
Erik R P Zuiderweg
Gordon M Crippen
Matthew Revington
Yongbo Zhang
P2860
P2888
P304
P356
10.1007/S10858-010-9403-2
P577
2010-03-16T00:00:00Z