Protonation state of E71 in KcsA and its role for channel collapse and inactivation.
about
Molecular pathophysiology and pharmacology of the voltage-sensing module of neuronal ion channelsProbing the energy landscape of activation gating of the bacterial potassium channel KcsALipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.Solid state NMR: The essential technology for helical membrane protein structural characterization.Membrane protein structural validation by oriented sample solid-state NMR: diacylglycerol kinase.Combination of ¹⁵N reverse labeling and afterglow spectroscopy for assigning membrane protein spectra by magic-angle-spinning solid-state NMR: application to the multidrug resistance protein EmrESolid state NMR and protein-protein interactions in membranesIon-binding properties of a K+ channel selectivity filter in different conformations.Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.Individual Ion Binding Sites in the K(+) Channel Play Distinct Roles in C-type Inactivation and in Recovery from Inactivation.Dynamic interaction between membrane-bound full-length cytochrome P450 and cytochrome b5 observed by solid-state NMR spectroscopyConformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.Semisynthetic K+ channels show that the constricted conformation of the selectivity filter is not the C-type inactivated state.Preparation of uniformly isotope labeled KcsA for solid state NMR: expression, purification, reconstitution into liposomes and functional assay.Transmembrane allosteric coupling of the gates in a potassium channel.Dynamics transitions at the outer vestibule of the KcsA potassium channel during gating.Determinants of pore folding in potassium channel biogenesis.Transmembrane allosteric energetics characterization for strong coupling between proton and potassium ion binding in the KcsA channel.Nuclear magnetic resonance (NMR) applied to membrane-protein complexes.Transmembrane Interactions of Full-length Mammalian Bitopic Cytochrome-P450-Cytochrome-b5 Complex in Lipid Bilayers Revealed by Sensitivity-Enhanced Dynamic Nuclear Polarization Solid-state NMR Spectroscopy.Shortening spin-lattice relaxation using a copper-chelated lipid at low-temperatures - A magic angle spinning solid-state NMR study on a membrane-bound protein.Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization.Proton-Based Structural Analysis of a Heptahelical Transmembrane Protein in Lipid Bilayers.The gating cycle of a K+ channel at atomic resolution.Chemical substitutions in the selectivity filter of potassium channels do not rule out constricted-like conformations for C-type inactivation.A single NaK channel conformation is not enough for non-selective ion conduction.Probing Conformational Changes during the Gating Cycle of a Potassium Channel in Lipid Bilayers.Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.
P2860
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P2860
Protonation state of E71 in KcsA and its role for channel collapse and inactivation.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Protonation state of E71 in KcsA and its role for channel collapse and inactivation.
@ast
Protonation state of E71 in KcsA and its role for channel collapse and inactivation.
@en
type
label
Protonation state of E71 in KcsA and its role for channel collapse and inactivation.
@ast
Protonation state of E71 in KcsA and its role for channel collapse and inactivation.
@en
prefLabel
Protonation state of E71 in KcsA and its role for channel collapse and inactivation.
@ast
Protonation state of E71 in KcsA and its role for channel collapse and inactivation.
@en
P2860
P356
P1476
Protonation state of E71 in KcsA and its role for channel collapse and inactivation.
@en
P2093
Manasi P Bhate
P2860
P304
15265-15270
P356
10.1073/PNAS.1211900109
P407
P577
2012-08-31T00:00:00Z