Assignment of the 1H nuclear magnetic resonance spectrum of the trypsin inhibitor E from Dendroaspis polylepis polylepis: Two-dimensional nuclear magnetic resonance at 500 MHz

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The assignment of the 1H nuclear magnetic resonance spectrum of the trypsin inhibitor E from the venom of Dendroaspis polylepis polylepis is described and documented. A sample of 18 mg of the protein was investigated with two-dimensional nuclear magnetic resonance experiments at 500 MHz. The assignments are based entirely on the amino acid sequence and the nuclear magnetic resonance data. Individual assignments were obtained for the backbone and C β protons of all 59 residues of inhibitor E, with the exceptions of the N-terminal amino group, Pro8, Pro13 and the amide proton of Gly37. The amino acid side-chain resonance assignments are complete, with the exception of Pro8, Pro13, C γH 2 of Glu49, all the lysyl and arginyl residues and the three histidyl residues 1, 34 and 53, for which the imidazole ring proton lines have not been assigned individually. The chemical shifts for the assigned resonances are listed for an aqueous solution at 50 °C and pH 3.2.