Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry.
about
The diverse and expanding role of mass spectrometry in structural and molecular biologyNanospray HX-MS configuration for structural interrogation of large protein systems.Catalytic robustness and torque generation of the F1-ATPaseLigand-induced conformational dynamics of the Escherichia coli Na+/H+ antiporter NhaA revealed by hydrogen/deuterium exchange mass spectrometry.
P2860
Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry.
description
2016 nî lūn-bûn
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2016年の論文
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2016年論文
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2016年論文
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2016年論文
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2016年論文
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2016年論文
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2016年论文
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name
Load-dependent destabilization ...... um-exchange mass spectrometry.
@ast
Load-dependent destabilization ...... um-exchange mass spectrometry.
@en
type
label
Load-dependent destabilization ...... um-exchange mass spectrometry.
@ast
Load-dependent destabilization ...... um-exchange mass spectrometry.
@en
prefLabel
Load-dependent destabilization ...... um-exchange mass spectrometry.
@ast
Load-dependent destabilization ...... um-exchange mass spectrometry.
@en
P2093
P2860
P356
P1476
Load-dependent destabilization ...... ium-exchange mass spectrometry
@en
P2093
Lars Konermann
Stanley D Dunn
P2860
P304
P356
10.1073/PNAS.1520464113
P407
P577
2016-02-16T00:00:00Z