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Resonance assignments of the ~1H spectrum of insulin are the basis on which to investi-gate its solution conformation by using NMR method. Owing to the complicated aggregationbehaviour of the molecule to give broadened n. m. r. lines, only limited resonance assignmentshave been reported. S-sulfonated A and B chains of insulin gave ~1H spectra with good reso-lutions. Based on the 500 MHz absolute 2D-COSY spectrum and 400 MHz phase sensitiveDQF-COSY, Relayed-COSY and NOESY spectra of B chain recorded in D_2O, all of thespin system identifications of the non-labile protons in the S-sulfonated B chain of insulinwere reported including the specific resonance assignments of eight residues: B_3Asn, B_9Ser,B_(16)Tyr, B_(22)Arg, B_(26)Tyr, B_(27)Thr, B_(28)Pro and B_(29)Lys. The pK values of B_(16) and B_(26) tyrosineare 10.65 and 10.60 respectively from pH titration.
Resonance assignments of the ~ 1H spectrum of insulin are the basis on which to instisti-gate its solution conformation by using NMR method. Owing to the complicated aggregation behavior of the molecule to give broadened nmr lines, only limited resonance assignments have been reported. S-sulfonated A and B chains of insulin gave ~ 1H spectra with good reso lutions. Based on the 500 MHz absolute 2D-COZY spectrum and 400 MHz phase sensitive DQF-COZY, Relayed-COZY and NOESY spectra of B chain recorded in D_2O, all of thespin system identifications of the non-labile protons in the S-sulfonated B chain of insulinwere reports including the specific resonance assignments of eight residues: B_3Asn, B_9Ser, B_ (16) Tyr, B_22Arg, B_26 Tyr, B_ (27) Thr, B 28 Pro and B 29 Lys. The pK values of B 16 and B 26 tyrosineare 10.65 and 10.60 respectively from pH titration.