Protonation and hydrogen bonding of Ca2+ site residues in the E2P phosphoenzyme intermediate of sarc...
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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United States: The Biophysical Society
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English
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United States: The Biophysical Society
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Protonation of the Ca(2+) ligands of the SR Ca(2+)-ATPase (SERCA1a) was studied by a combination of rapid scan FTIR spectroscopy and electrostatic calculations. With FTIR spectroscopy, we investigated the pH dependence of C=O bands of the Ca(2+)-free phosphoenzyme (E2P) and obtained direct experimental evidence for the protonation of carboxyl group...
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Full title
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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TN_cdi_swepub_primary_oai_DiVA_org_su_14844
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_su_14844
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ISSN
0006-3495,1542-0086
E-ISSN
1542-0086
DOI
10.1529/biophysj.107.114033
