Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation EPR - Wikidata - awgldk - TriplyDB

Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation EPR

Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation EPR

http://www.wikidata.org/entity/Q34351236

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NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.Electron spin-echo envelope modulation (ESEEM) reveals water and phosphate interactions with the KcsA potassium channel.Accessibility and dynamics of nitroxide side chains in T4 lysozyme measured by saturation recovery EPR.De novo high-resolution protein structure determination from sparse spin-labeling EPR data.Probing Protein Secondary Structure using EPR: Investigating a Dynamic Region of Visual Arrestin.Navigating Membrane Protein Structure, Dynamics, and Energy Landscapes Using Spin Labeling and EPR Spectroscopy.Cooperative Substrate-Cofactor Interactions and Membrane Localization of the Bacterial Phospholipase A2 (PLA2) Enzyme, ExoU.Toward the fourth dimension of membrane protein structure: insight into dynamics from spin-labeling EPR spectroscopy Resolving Conformational and Rotameric Exchange in Spin-Labeled Proteins Using Saturation Recovery EPR The activated state of a sodium channel voltage sensor in a membrane environment Lipid composition regulates the orientation of transmembrane helices in HorA, an ABC multidrug transporter.Electron paramagnetic resonance spectroscopy of nitroxide-labeled calmodulin.Structure, dynamics, and substrate-induced conformational changes of the multidrug transporter EmrE in liposomes.Ion/substrate-dependent conformational dynamics of a bacterial homolog of neurotransmitter:sodium symporters.Studies of the mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes Hierarchical organization in the amyloid core of yeast prion protein Ure2.Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain.Site-directed spin labeling of proteins for distance measurements in vitro and in cells.A chimeric prokaryotic pentameric ligand-gated channel reveals distinct pathways of activation.In Vitro Demonstration of Dual Light-Driven Na⁺/H⁺ Pumping by a Microbial Rhodopsin.A paramagnetic molecular voltmeter.Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN(-) binding defined by EPR-based hybrid method.Interaction of Spin-Labeled Lipid Membranes with Transition Metal Ions.Selective Membrane Disruption Mechanism of an Antibacterial γ-AApeptide Defined by EPR Spectroscopy.Demonstration of short-lived complexes of cytochrome c with cytochrome bc1 by EPR spectroscopy: implications for the mechanism of interprotein electron transfer.Actin-binding cleft closure in myosin II probed by site-directed spin labeling and pulsed EPR.Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels Structure and pH-induced structural rearrangements of the putative multidrug efflux pump EmrD in liposomes probed by site-directed spin labeling.Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA.The role of arrestin alpha-helix I in receptor binding.Triplet state of the semiquinone-Rieske cluster as an intermediate of electronic bifurcation catalyzed by cytochrome bc1.Crystal structure and dynamics of a lipid-induced potential desensitized-state of a pentameric ligand-gated channel.EPR Studies of Gating Mechanisms in Ion Channels.Characterizing rhodopsin signaling by EPR spectroscopy: from structure to dynamics.Elucidation of inositol hexaphosphate and heparin interaction sites and conformational changes in arrestin-1 by solution nuclear magnetic resonance.Structural basis for allosteric coupling at the membrane-protein interface in Gloeobacter violaceus ligand-gated ion channel (GLIC).Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers.Desensitization mechanism in prokaryotic ligand-gated ion channel Conformational transitions underlying pore opening and desensitization in membrane-embedded Gloeobacter violaceus ligand-gated ion channel (GLIC)Molecular details of Bax activation, oligomerization, and membrane insertion.

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P2860

Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation EPR

http://www.wikidata.org/entity/Q34351236

description

2005 nî lūn-bûn

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2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2005 թվականի հուլիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Accessibility of nitroxide sid ...... ates from power saturation EPR

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Accessibility of nitroxide sid ...... ates from power saturation EPR

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Accessibility of nitroxide sid ...... ates from power saturation EPR

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Accessibility of nitroxide sid ...... ates from power saturation EPR

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Accessibility of nitroxide sid ...... ates from power saturation EPR

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Accessibility of nitroxide sid ...... ates from power saturation EPR

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Accessibility of nitroxide sid ...... ates from power saturation EPR

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Accessibility of nitroxide sid ...... ates from power saturation EPR

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Accessibility of nitroxide sid ...... ates from power saturation EPR

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BIOPHYSJ.105.059063

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Biophysical Journal

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Accessibility of nitroxide sid ...... ates from power saturation EPR

@en

P2093

Christian Altenbach

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

Hassane McHaourab

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Roy Hemker

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Wayne L Hubbell

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P2860

The interpretation of protein structures: estimation of static accessibility

MOLMOL: a program for display and analysis of macromolecular structures

Nitroxide spin-spin interactions: applications to protein structure and dynamics.

Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations.

Accessibility and dynamics of nitroxide side chains in T4 lysozyme measured by saturation recovery EPR.

Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants.

Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics.

Determination of the distance between two spin labels attached to a macromolecule.

Identifying conformational changes with site-directed spin labeling.

Using nitroxide spin labels. How to obtain T1e from continuous wave electron paramagnetic resonance spectra at all rotational rates.

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2103-2112

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scholarly article

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10.1529/BIOPHYSJ.105.059063

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3

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89

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Wojciech Froncisz

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2005-07-01T00:00:00Z

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7749107

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15994891

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1366712

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