Protonation and hydrogen bonding of Ca2+ site residues in the E2P phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations.
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Distinctive features of catalytic and transport mechanisms in mammalian sarco-endoplasmic reticulum Ca2+ ATPase (SERCA) and Cu+ (ATP7A/B) ATPasesProtonation of key acidic residues is critical for the K⁺-selectivity of the Na/K pump.The Ca2+-ATPase pump facilitates bidirectional proton transport across the sarco/endoplasmic reticulum.Structural changes in the catalytic cycle of the Na+,K+-ATPase studied by infrared spectroscopy.Conformational changes of recombinant Ca2+-ATPase studied by reaction-induced infrared difference spectroscopy.
P2860
Protonation and hydrogen bonding of Ca2+ site residues in the E2P phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations.
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2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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name
Protonation and hydrogen bondi ...... nd electrostatic calculations.
@ast
Protonation and hydrogen bondi ...... nd electrostatic calculations.
@en
type
label
Protonation and hydrogen bondi ...... nd electrostatic calculations.
@ast
Protonation and hydrogen bondi ...... nd electrostatic calculations.
@en
prefLabel
Protonation and hydrogen bondi ...... nd electrostatic calculations.
@ast
Protonation and hydrogen bondi ...... nd electrostatic calculations.
@en
P2093
P2860
P1433
P1476
Protonation and hydrogen bondi ...... and electrostatic calculations
@en
P2093
Eeva-Liisa Karjalainen
Julia Andersson
Karin Hauser
P2860
P304
P356
10.1529/BIOPHYSJ.107.114033
P407
P577
2007-09-21T00:00:00Z