Ion mobility-mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility.
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Native Mass Spectrometry in Fragment-Based Drug DiscoveryCryo-EM studies of the structure and dynamics of vacuolar-type ATPasesThe emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes.Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPaseIdentifying and Visualizing Macromolecular Flexibility in Structural BiologySurface Accessibility and Dynamics of Macromolecular Assemblies Probed by Covalent Labeling Mass Spectrometry and Integrative ModelingAmphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase.Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA.Native-Like and Denatured Cytochrome c Ions Yield Cation-to-Anion Proton Transfer Reaction Products with Similar Collision Cross-Sections.Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonanceStructure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.Topological models of heteromeric protein assemblies from mass spectrometry: application to the yeast eIF3:eIF5 complexSalt Bridge Rearrangement (SaBRe) Explains the Dissociation Behavior of Noncovalent ComplexesThe study of vacuolar-type ATPases by single particle electron microscopy.Assembling the pieces of macromolecular complexes: Hybrid structural biology approaches.Coming to Grips with Ambiguity: Ion Mobility-Mass Spectrometry for Protein Quaternary Structure Assignment.Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS.Charge reduction stabilizes intact membrane protein complexes for mass spectrometry.Topological Dissection of the Membrane Transport Protein Mhp1 Derived from Cysteine Accessibility and Mass Spectrometry.Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS.Characterization of the flexibility of the peripheral stalk of prokaryotic rotary A-ATPases by atomistic simulations.Ligand binding to a G protein-coupled receptor captured in a mass spectrometer.Ion mobility mass spectrometry of peptide, protein, and protein complex ions using a radio-frequency confining drift cell.Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease.Lipids Shape the Electron Acceptor-Binding Site of the Peripheral Membrane Protein Dihydroorotate Dehydrogenase.Interpreting the Collision Cross Sections of Native-like Protein Ions: Insights from Cation-to-Anion Proton-Transfer Reactions.Characterization of Conformational Ensembles of Protonated N-glycans in the Gas-Phase.Radio-Frequency (rf) Confinement in Ion Mobility Spectrometry: Apparent Mobilities and Effective Temperatures.
P2860
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P2860
Ion mobility-mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility.
description
2014 nî lūn-bûn
@nan
2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年學術文章
@yue
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2014年學術文章
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name
Ion mobility-mass spectrometry ...... in conformational flexibility.
@en
type
label
Ion mobility-mass spectrometry ...... in conformational flexibility.
@en
prefLabel
Ion mobility-mass spectrometry ...... in conformational flexibility.
@en
P2093
P2860
P356
P1433
P1476
Ion mobility-mass spectrometry ...... in conformational flexibility.
@en
P2093
Argyris Politis
Daniela Stock
Idlir Liko
Kuan-Jung Wu
Roberta Davies
P2860
P2888
P304
P356
10.1038/NCHEM.1868
P577
2014-02-16T00:00:00Z