دورية أكاديمية
1H NMR study of robustoxin, the lethal neurotoxin from the funnel web spider Atrax robustus.
| العنوان: | 1H NMR study of robustoxin, the lethal neurotoxin from the funnel web spider Atrax robustus. |
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| المؤلفون: | Temple MD; School of Biochemistry and Molecular Genetics, University of New South Wales, Sydney, Australia., Hinds MG, Sheumack DD, Howden ME, Norton RS |
| المصدر: | Toxicon : official journal of the International Society on Toxinology [Toxicon] 1999 Mar; Vol. 37 (3), pp. 485-506. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Pergamon Press Country of Publication: England NLM ID: 1307333 Publication Model: Print Cited Medium: Print ISSN: 0041-0101 (Print) Linking ISSN: 00410101 NLM ISO Abbreviation: Toxicon Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Oxford ; New York : Pergamon Press, c1962- |
| مواضيع طبية MeSH: | Neurotoxins/*chemistry , Peptides/*chemistry , Spider Venoms/*chemistry , Spiders/*metabolism, Amino Acid Sequence ; Animals ; Hydrogen ; Hydrogen-Ion Concentration ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Protein Structure, Secondary |
| مستخلص: | Robustoxin, the lethal neurotoxin from the Sydney funnel web spider Atrax robustus, is a polypeptide of 42 residues cross-linked by four disulfide bonds. This paper describes the sequence-specific assignment of resonances in the 1H nuclear magnetic resonance spectrum of robustoxin in aqueous solution. Several broad backbone amide resonances were encountered in spectra recorded at 27 degrees C, making the assignments at that temperature incomplete. In spectra recorded at lower temperatures these amide resonances became sharper, but others that were sharp at 27 degrees C became broad, indicative of conformational averaging on the millisecond timescale for certain regions of the structure. Nevertheless, it was possible to establish that robustoxin contains a small, triple-stranded, antiparallel beta-sheet and several reverse turns, but no alpha-helix. These observations indicate that this toxin may adopt the inhibitor cystine knot structure found in polypeptides from a diverse range of species, including a number of spiders. Analysis of the pH dependence of the spectrum yielded pKa values for Tyr22 and Tyr25, one of the three carboxyl groups, and the Lys residues. |
| المشرفين على المادة: | 0 (Neurotoxins) 0 (Peptides) 0 (Spider Venoms) 7YNJ3PO35Z (Hydrogen) 91728-12-0 (robustoxin) |
| تواريخ الأحداث: | Date Created: 19990318 Date Completed: 19990623 Latest Revision: 20190822 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1016/s0041-0101(98)00186-x |
| PMID: | 10080353 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 0041-0101 |
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| DOI: | 10.1016/s0041-0101(98)00186-x |