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A conformational analysis in water and DMSO of two tachykinin family peptides (scyliorhinin I (ScyI) and scyliorhinin II (ScyII)) was carried out by 1D and 2D NMR (DQF-COSY, TOCSY, HMQC, HMBC, NOESY and ROESY) and molecular dynamics calculation methods. In DMSO, two groups of conformations (major and minor) were obtained for both peptides based on the experimental data. The conformations proposed for ScyI represent a folded structure, which shows certain similarities to the structures reported for other NK-1 and NK-2 tachykinin agonists. In water ScyII displays a flexible, extended structure, whereas in DMSO the structure is more compact and, in the fragment from the centre to the C-terminus, several -turns may be present. 相似文献
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Rodziewicz Sylwia Qi Xiao-Fei Rolka Krzysztof 《International journal of peptide research and therapeutics》1998,5(5-6):429-432
Summary A conformational analysis in water and DMSO of two tachykinin family peptides (scyliorhinin I (ScyI) and scyliorhinin II (ScyII))
was carried out by 1D and 2D NMR (DQF-COSY, TOCSY, HMQC, HMBC, NOESY and ROESY) and molecular dynamics calculation methods.
In DMSO, two groups of conformations (major and minor) were obtained for both peptides based on the experimental data. The
conformations proposed for ScyI represent a folded structure, which shows certain similarities to the structures reported
for other NK-1 and NK-2 tachykinin agonists. In water ScyII displays a flexible, extended structure, whereas in DMSO the structure
is more compact and, in the fragment from the centre to the C-terminus, several β-turns may be present. 相似文献
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