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An ω1-band-selective, ω1-homonuclear decoupled ROESY experiment: application to the assignment of 1H NMR spectra of difficult-to-assign peptide sequences

✍ Scribed by Andreas Kaerner; Dallas L. Rabenstein

Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
309 KB
Volume
36
Category
Article
ISSN
0749-1581

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✦ Synopsis

Application of an decoupled ROESY (BASHD-ROESY) experi-u 1 -band-selective, u 1 -homonuclear ment to the assignment of 1H NMR spectra of peptides is demonstrated. Band selection in the dimension is u 1 achieved with the double pulsed Ðeld gradient spin echo (DPFGSE) technique ; homonuclear decoupling in the u 1 dimension is achieved by placing a non-selective 180¡ pulse together with the Ðrst half of the DPFGSE in the middle of the evolution period. Application of the BASHD-ROESY experiment is demonstrated with the complete assignment of the proton resonances of the synthetic 19 amino acid peptide N-AcÈAlaÈGluÈAlaÈAlaÈ AlaÈArgÈ AlaÈAlaÈAlaÈArgÈArgÈAlaÈAlaÈ Critical to making the assignments was the ArgÈArgÈAlaÈAlaÈAlaÈArgÈNH 2 . signiÐcantly increased resolution in the region of the ROESY spectrum measured with the BASHD-C a HÈNH ROESY pulse sequence with band selection and homonuclear decoupling in the region. NOEs observed for C a H the peptide indicate it has a helical secondary structure in solution.

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## Abstract Two‐dimensional ^1^H NMR experiments that achieve band‐selective, homonuclear decoupling in both the indirectly detected F1 and directly detected F2 dimensions were used to assign the highly overlapped ^1^H NMR spectrum of the peptide Ac‐SRGKARVRAKVKDQTK‐NH~2~, both free in solution and