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https://hdl.handle.net/2440/53520
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dc.contributor.author | Pukala, T. | - |
dc.contributor.author | Urathamakul, T. | - |
dc.contributor.author | Watt, S. | - |
dc.contributor.author | Beck, J. | - |
dc.contributor.author | Jackway, R. | - |
dc.contributor.author | Bowie, J. | - |
dc.date.issued | 2008 | - |
dc.identifier.citation | Rapid Communications in Mass Spectrometry, 2008; 22(22):3501-3509 | - |
dc.identifier.issn | 0951-4198 | - |
dc.identifier.issn | 1097-0231 | - |
dc.identifier.uri | http://hdl.handle.net/2440/53520 | - |
dc.description.abstract | Amphibian peptides which inhibit the formation of nitric oxide by neuronal nitric oxide synthase (nNOS) do so by binding to the protein cofactor, Ca2+calmodulin (Ca2+CaM). Complex formation between active peptides and Ca2+CaM has been demonstrated by negative ion electrospray ionisation mass spectrometry using an aqueous ammonium acetate buffer system. In all cases studied, the assemblies are formed with a 1:1:4 calmodulin/peptide/Ca2+ stoichiometry. In contrast, the complex involving the 20-residue binding domain of the plasma Ca2+ pump C20W (LRRGQILWFRGLNRIQTQIK-OH) with CaM has been shown by previous two-dimensional nuclear magnetic resonance (2D NMR) studies to involve complexation of the C-terminal end of CaM. Under identical conditions to those used for the amphibian peptide study, the ESI complex between C20W and CaM shows specific 1:1:2 stoichiometry. Since complex formation with the studied amphibian peptides requires Ca2+CaM to contain its full complement of four Ca2+ ions, this indicates that the amphibian peptides require both ends of the CaM to effect complex formation. Charge-state analysis and an H/D exchange experiment (with caerin 1.8) suggest that complexation involves Ca2+CaM undergoing a conformational change to a more compact structure. | - |
dc.description.statementofresponsibility | Tara L. Pukala, Thitima Urathamakul, Stephen J. Watt, Jennifer L. Beck, Rebecca J. Jackway, John H. Bowie | - |
dc.language.iso | en | - |
dc.publisher | John Wiley & Sons Ltd | - |
dc.rights | © 2008 John Wiley & Sons, Ltd. | - |
dc.source.uri | http://dx.doi.org/10.1002/rcm.3757 | - |
dc.subject | Animals | - |
dc.subject | Anura | - |
dc.subject | Calcium | - |
dc.subject | Peptides | - |
dc.subject | Amphibian Proteins | - |
dc.subject | Calmodulin | - |
dc.subject | Spectrometry, Mass, Electrospray Ionization | - |
dc.subject | Binding Sites | - |
dc.subject | Protein Binding | - |
dc.subject | Nitric Oxide Synthase Type I | - |
dc.title | Binding studies of nNOS-active amphibian peptides and Ca²⁺ calmodulin, using negative ion electrospray ionisation mass spectrometry | - |
dc.title.alternative | Binding studies of nNOS-active amphibian peptides and Ca(2+) calmodulin, using negative ion electrospray ionisation mass spectrometry | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1002/rcm.3757 | - |
dc.relation.grant | ARC | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Pukala, T. [0000-0001-7391-1436] | - |
Appears in Collections: | Aurora harvest Chemistry publications |
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