Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes - Wikidata - awgldk - TriplyDB

Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes

Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes

http://www.wikidata.org/entity/Q38120224

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Prediction of Protein Structure Using Surface Accessibility Data RNA structure refinement using NMR solvent accessibility data.Implications of the differing roles of the β1 and β3 transmembrane and cytoplasmic domains for integrin function.Structural and Dynamic Insights of the Interaction between Tritrpticin and Micelles: An NMR Study.Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide.Structural and functional implications of the interaction between macrolide antibiotics and bile acids A new role for FBP21 as regulator of Brr2 helicase activity.Characterization of Protein-Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements.Allosteric modulation of peroxisomal membrane protein recognition by farnesylation of the peroxisomal import receptor PEX19.Paramagnetic Ligand Tagging To Identify Protein Binding Sites.Investigating Protein-Ligand Interactions by Solution Nuclear Magnetic Resonance Spectroscopy.Protein Structural Ensembles Visualized by Solvent Paramagnetic Relaxation Enhancement.Theory and practice of using solvent paramagnetic relaxation enhancement to characterize protein conformational dynamics.Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme Catalysis NMR-based structural biology enhanced by dynamic nuclear polarization at high magnetic field

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P2860

Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes

http://www.wikidata.org/entity/Q38120224

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article científic

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article scientifique

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artigo científico

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artigo científico

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artikel ilmiah

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artikull shkencor

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artículo científico

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name

Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes

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type

label

Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes

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prefLabel

Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes

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Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes

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Henry G Hocking

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Creative Commons Attribution-NonCommercial 3.0 Unported

P2860

Relaxation Processes in a System of Two Spins

Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer

NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model

Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves

Positioning of micelle-bound peptides by paramagnetic relaxation enhancements

Use of relaxation enhancements in a paramagnetic environment for the structure determination of proteins using NMR spectroscopy

Structural Basis for Homodimerization of the Src-associated during Mitosis, 68-kDa Protein (Sam68) Qua1 Domain

Solution Structure and Membrane Binding of the Toxin Fst of the par Addiction Module

Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins

ARIA: automated NOE assignment and NMR structure calculation

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3082-3094

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scholarly article

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10.1002/CPHC.201300219

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