Proton NMR resonance assignments and surface accessibility of tryptophan residues of a dimeric phospholipase A2 from Trimeresurus flavoviridis |
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Authors: | T Endo M Oya R Kaptein G W Vuister H Kihara N Mohri S Tanaka M Ohno |
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Institution: | Department of Chemistry, College of Technology, Gunma University, Kiryu, Japan. |
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Abstract: | Proton NMR spectra of a dimeric phospholipase A2 from Trimeresurus flavoviridis have been recorded. N-1 proton resonances of the tryptophan indole rings have been detected and assigned to specific positions, Trp-3/Trp-30, Trp-68 and Trp-108, by comparing the spectra of the enzyme derivatives with tryptophans oxidized to differing extents. Photo-CIDNP experiments have revealed that Trp-68 and Trp-108 are exposed while Trp-3 and Trp-30 are buried in the molecule. This is consistent with the X-ray crystal structure of a homologous phospholipase A2 from Crotalus atrox where residues 3 and 30 are located at a dimer interface, but inconsistent with the results of stepwise oxidation of tryptophan residues. |
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Keywords: | Phospholipase A2 Tryptophan 1H-NMR Photo-CIDNP Surface accessibility N-Bromosuccinimide oxidation |
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