
We characterize thus-far elusive domain rearrangements of a calcium-transporting ATPase in the native membrane.
CONFORMATIONAL-CHANGES, Protein Conformation, Atom and Molecular Physics and Optics, PUMP, STRUCTURAL DYNAMICS, Quantitative Structure-Activity Relationship, Molecular Dynamics Simulation, CA2+-ATPASE, Crystallography, X-Ray, Sarcoplasmic Reticulum Calcium-Transporting ATPases, PHOSPHOENZYME, ATPase, Protein Interaction Domains and Motifs, time-resolved X-ray solution scattering, Research Articles, Ion Transport, SARCOPLASMIC-RETICULUM, Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin), Kinetics, ATPase, time-resolved X-ray solution scattering, MOLECULAR-DYNAMICS, SKELETAL-MUSCLE, Atom- och molekylfysik och optik, Calcium, MEMBRANE, CALCIUM-TRANSPORT, Protein Binding
CONFORMATIONAL-CHANGES, Protein Conformation, Atom and Molecular Physics and Optics, PUMP, STRUCTURAL DYNAMICS, Quantitative Structure-Activity Relationship, Molecular Dynamics Simulation, CA2+-ATPASE, Crystallography, X-Ray, Sarcoplasmic Reticulum Calcium-Transporting ATPases, PHOSPHOENZYME, ATPase, Protein Interaction Domains and Motifs, time-resolved X-ray solution scattering, Research Articles, Ion Transport, SARCOPLASMIC-RETICULUM, Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin), Kinetics, ATPase, time-resolved X-ray solution scattering, MOLECULAR-DYNAMICS, SKELETAL-MUSCLE, Atom- och molekylfysik och optik, Calcium, MEMBRANE, CALCIUM-TRANSPORT, Protein Binding
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