Flexible membrane proteins: functional dynamics captured by mass spectrometry (Q26849927)

language of work or name

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October 2014

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Current Opinion in Structural Biology

published in

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volume

28

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page(s)

122-30

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describes a project that uses

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Hydrogen exchange mass spectrometry for the analysis of protein dynamics

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https://api.crossref.org/works/10.1016%2FJ.SBI.2014.08.005

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Mass spectrometry combined with oxidative labeling for exploring protein structure and folding.

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Crosslinking combined with mass spectrometry for structural proteomics

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Chemical cross-linkers for protein structure studies by mass spectrometry

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Electron spin resonance in membrane research: protein-lipid interactions from challenging beginnings to state of the art.

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Membrane-mediated protein-protein interactions and connection to elastic models: a coarse-grained simulation analysis of gramicidin A association

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Protein complexes are under evolutionary selection to assemble via ordered pathways

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Structure and activity of the RNA-targeting Type III-B CRISPR-Cas complex of Thermus thermophilus

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Overcoming the challenges of membrane protein crystallography.

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Protein folding mechanisms studied by pulsed oxidative labeling and mass spectrometry

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Showcasing modern molecular dynamics simulations of membrane proteins through G protein-coupled receptors

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Linking structural change with functional regulation-insights from mass spectrometry

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Membrane protein structure determination by electron crystallography

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Mass spectrometry supported determination of protein complex structure

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Conformational changes during the gating of a potassium channel revealed by structural mass spectrometry

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Ligand-dependent perturbation of the conformational ensemble for the GPCR β2 adrenergic receptor revealed by HDX.

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Crystal Structure of the Yeast Vacuolar ATPase Heterotrimeric EGChead Peripheral Stalk Complex

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The role of lipids in defining membrane protein interactions: insights from mass spectrometry

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Structural proteomics of macromolecular assemblies using oxidative footprinting and mass spectrometry

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When proteomics meets structural biology

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Structural divergence of the rotary ATPases

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Direct ionization of large proteins and protein complexes by desorption electrospray ionization-mass spectrometry

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Fragmentation of integral membrane proteins in the gas phase

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Dynamics of the beta2-adrenergic G-protein coupled receptor revealed by hydrogen-deuterium exchange

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Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry

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Conformational Changes in the G Protein-Coupled Receptor Rhodopsin Revealed by Histidine Hydrogen−Deuterium Exchange

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Ion Mobility Mass Spectrometry of Two Tetrameric Membrane Protein Complexes Reveals Compact Structures and Differences in Stability and Packing

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Detergent release prolongs the lifetime of native-like membrane protein conformations in the gas-phase.

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Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase

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Structure of a bacterial multidrug ABC transporter

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Crystal structure of the β2 adrenergic receptor-Gs protein complex

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Conformational changes in the G protein Gs induced by the β2 adrenergic receptor

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Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans

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Molecular signatures of G-protein-coupled receptors

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Transport dynamics in a glutamate transporter homologue.

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Structural basis of the alternating-access mechanism in a bile acid transporter

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Membrane proteins bind lipids selectively to modulate their structure and function.

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Ion mobility-mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility

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The dynamic stator stalk of rotary ATPases

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Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation.

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Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions

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Detergent-free mass spectrometry of membrane protein complexes.

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Ion mobility–mass spectrometry analysis of large protein complexes

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Mass spectrometry of intact membrane protein complexes

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Towards a structural view of gating in potassium channels

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Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation

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X-ray crystal structure of voltage-gated proton channel

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Conformational dynamics of ligand-dependent alternating access in LeuT.

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Membrane protein structural insights from chemical labeling and mass spectrometry

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Hydrogen exchange mass spectrometry for studying protein structure and dynamics

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Lipid-protein interactions as determinants of membrane protein structure and function

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Flexibility in the ABC transporter MsbA: Alternating access with a twist

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The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex

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Dynamics of a bacterial multidrug ABC transporter in the inward- and outward-facing conformations

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Kinetics of prephosphorylation reactions and myosin light chain phosphorylation in smooth muscle. Flash photolysis studies with caged calcium and caged ATP.

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Dynamic protein ligand interactions--insights from MS.

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A tridecameric c ring of the adenosine triphosphate (ATP) synthase from the thermoalkaliphilic Bacillus sp. strain TA2.A1 facilitates ATP synthesis at low electrochemical proton potential

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Turnover number of Escherichia coli F0F1 ATP synthase for ATP synthesis in membrane vesicles.

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High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor

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Micelles protect membrane complexes from solution to vacuum.

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Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding

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Biomolecule analysis by ion mobility spectrometry

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G protein mechanisms: insights from structural analysis

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Membrane protein structure and dynamics from NMR spectroscopy

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Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin

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The C-H peripheral stalk base: a novel component in V1-ATPase assembly

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