$ Sequential^{1} $H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins
Abstract The complete sequence-specific assignment of resonances in $ the^{1} $H-NMR spectrum of the polypeptide neurotoxin III (Hm III) from the sea anemoneHeteractis macrodactylus is described. Comparison of the chemical shifts and pattern of NOEs for Hm III with those for the related toxin Hp III...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Hinds, Mark G. [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1993 |
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| Anmerkung: |
© Plenum Publishing Corporation 1993 |
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| Übergeordnetes Werk: |
Enthalten in: The protein journal - Dordrecht : Springer Science + Business Media B.V., 2004, 12(1993), 3 vom: 01. Juni, Seite 371-378 |
|---|---|
| Übergeordnetes Werk: |
volume:12 ; year:1993 ; number:3 ; day:01 ; month:06 ; pages:371-378 |
| Links: |
|---|
| DOI / URN: |
10.1007/BF01028199 |
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SPR052838730 |
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| 245 | 1 | 0 | |a $ Sequential^{1} $H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins |
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| 520 | |a Abstract The complete sequence-specific assignment of resonances in $ the^{1} $H-NMR spectrum of the polypeptide neurotoxin III (Hm III) from the sea anemoneHeteractis macrodactylus is described. Comparison of the chemical shifts and pattern of NOEs for Hm III with those for the related toxin Hp III fromHeteractis paumotensis, which differs only in the substitution of Asn for Tyr at position 11, shows that the overall secondary and tertiary structures are conserved. The largest differences in chemical shift caused by the substitution at position 11 are observed for the NH resonances of Arg-13, Thr-14, Ala-15, Leu-17, and Cys-26. The $ C^{α} $H resonances influenced most are those of ASP-6, Gly-9, Leu-17, and Glu-42, while the most affected $ C^{β} $H resonances are from Leu-17, Glu-28, and Lys-32. The absence of long-range NOEs to the aromatic ring of Tyr-11 as well as the lack of significant chemical shift effects on residues outside the loop comprising residues 7–16 confirm that this part of the loop makes no long-lived contacts with the rest of the molecule. The deviations from random coil shifts of Hm III are compared with those of the related anemone toxins Hp II, Hp III, and toxin I fromStichodactyla helianthus (Sh I). The similarity in deviations in chemical shift as a function of sequence position for these four toxins emphasizes the overall structural homology among these polypeptides. | ||
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10.1007/BF01028199 doi (DE-627)SPR052838730 (SPR)BF01028199-e DE-627 ger DE-627 rakwb eng Hinds, Mark G. verfasserin aut $ Sequential^{1} $H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins 1993 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1993 Abstract The complete sequence-specific assignment of resonances in $ the^{1} $H-NMR spectrum of the polypeptide neurotoxin III (Hm III) from the sea anemoneHeteractis macrodactylus is described. Comparison of the chemical shifts and pattern of NOEs for Hm III with those for the related toxin Hp III fromHeteractis paumotensis, which differs only in the substitution of Asn for Tyr at position 11, shows that the overall secondary and tertiary structures are conserved. The largest differences in chemical shift caused by the substitution at position 11 are observed for the NH resonances of Arg-13, Thr-14, Ala-15, Leu-17, and Cys-26. The $ C^{α} $H resonances influenced most are those of ASP-6, Gly-9, Leu-17, and Glu-42, while the most affected $ C^{β} $H resonances are from Leu-17, Glu-28, and Lys-32. The absence of long-range NOEs to the aromatic ring of Tyr-11 as well as the lack of significant chemical shift effects on residues outside the loop comprising residues 7–16 confirm that this part of the loop makes no long-lived contacts with the rest of the molecule. The deviations from random coil shifts of Hm III are compared with those of the related anemone toxins Hp II, Hp III, and toxin I fromStichodactyla helianthus (Sh I). The similarity in deviations in chemical shift as a function of sequence position for these four toxins emphasizes the overall structural homology among these polypeptides. Norton, Raymond S. aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 12(1993), 3 vom: 01. Juni, Seite 371-378 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:12 year:1993 number:3 day:01 month:06 pages:371-378 https://dx.doi.org/10.1007/BF01028199 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 12 1993 3 01 06 371-378 |
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10.1007/BF01028199 doi (DE-627)SPR052838730 (SPR)BF01028199-e DE-627 ger DE-627 rakwb eng Hinds, Mark G. verfasserin aut $ Sequential^{1} $H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins 1993 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1993 Abstract The complete sequence-specific assignment of resonances in $ the^{1} $H-NMR spectrum of the polypeptide neurotoxin III (Hm III) from the sea anemoneHeteractis macrodactylus is described. Comparison of the chemical shifts and pattern of NOEs for Hm III with those for the related toxin Hp III fromHeteractis paumotensis, which differs only in the substitution of Asn for Tyr at position 11, shows that the overall secondary and tertiary structures are conserved. The largest differences in chemical shift caused by the substitution at position 11 are observed for the NH resonances of Arg-13, Thr-14, Ala-15, Leu-17, and Cys-26. The $ C^{α} $H resonances influenced most are those of ASP-6, Gly-9, Leu-17, and Glu-42, while the most affected $ C^{β} $H resonances are from Leu-17, Glu-28, and Lys-32. The absence of long-range NOEs to the aromatic ring of Tyr-11 as well as the lack of significant chemical shift effects on residues outside the loop comprising residues 7–16 confirm that this part of the loop makes no long-lived contacts with the rest of the molecule. The deviations from random coil shifts of Hm III are compared with those of the related anemone toxins Hp II, Hp III, and toxin I fromStichodactyla helianthus (Sh I). The similarity in deviations in chemical shift as a function of sequence position for these four toxins emphasizes the overall structural homology among these polypeptides. Norton, Raymond S. aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 12(1993), 3 vom: 01. Juni, Seite 371-378 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:12 year:1993 number:3 day:01 month:06 pages:371-378 https://dx.doi.org/10.1007/BF01028199 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 12 1993 3 01 06 371-378 |
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10.1007/BF01028199 doi (DE-627)SPR052838730 (SPR)BF01028199-e DE-627 ger DE-627 rakwb eng Hinds, Mark G. verfasserin aut $ Sequential^{1} $H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins 1993 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1993 Abstract The complete sequence-specific assignment of resonances in $ the^{1} $H-NMR spectrum of the polypeptide neurotoxin III (Hm III) from the sea anemoneHeteractis macrodactylus is described. Comparison of the chemical shifts and pattern of NOEs for Hm III with those for the related toxin Hp III fromHeteractis paumotensis, which differs only in the substitution of Asn for Tyr at position 11, shows that the overall secondary and tertiary structures are conserved. The largest differences in chemical shift caused by the substitution at position 11 are observed for the NH resonances of Arg-13, Thr-14, Ala-15, Leu-17, and Cys-26. The $ C^{α} $H resonances influenced most are those of ASP-6, Gly-9, Leu-17, and Glu-42, while the most affected $ C^{β} $H resonances are from Leu-17, Glu-28, and Lys-32. The absence of long-range NOEs to the aromatic ring of Tyr-11 as well as the lack of significant chemical shift effects on residues outside the loop comprising residues 7–16 confirm that this part of the loop makes no long-lived contacts with the rest of the molecule. The deviations from random coil shifts of Hm III are compared with those of the related anemone toxins Hp II, Hp III, and toxin I fromStichodactyla helianthus (Sh I). The similarity in deviations in chemical shift as a function of sequence position for these four toxins emphasizes the overall structural homology among these polypeptides. Norton, Raymond S. aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 12(1993), 3 vom: 01. Juni, Seite 371-378 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:12 year:1993 number:3 day:01 month:06 pages:371-378 https://dx.doi.org/10.1007/BF01028199 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 12 1993 3 01 06 371-378 |
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10.1007/BF01028199 doi (DE-627)SPR052838730 (SPR)BF01028199-e DE-627 ger DE-627 rakwb eng Hinds, Mark G. verfasserin aut $ Sequential^{1} $H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins 1993 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1993 Abstract The complete sequence-specific assignment of resonances in $ the^{1} $H-NMR spectrum of the polypeptide neurotoxin III (Hm III) from the sea anemoneHeteractis macrodactylus is described. Comparison of the chemical shifts and pattern of NOEs for Hm III with those for the related toxin Hp III fromHeteractis paumotensis, which differs only in the substitution of Asn for Tyr at position 11, shows that the overall secondary and tertiary structures are conserved. The largest differences in chemical shift caused by the substitution at position 11 are observed for the NH resonances of Arg-13, Thr-14, Ala-15, Leu-17, and Cys-26. The $ C^{α} $H resonances influenced most are those of ASP-6, Gly-9, Leu-17, and Glu-42, while the most affected $ C^{β} $H resonances are from Leu-17, Glu-28, and Lys-32. The absence of long-range NOEs to the aromatic ring of Tyr-11 as well as the lack of significant chemical shift effects on residues outside the loop comprising residues 7–16 confirm that this part of the loop makes no long-lived contacts with the rest of the molecule. The deviations from random coil shifts of Hm III are compared with those of the related anemone toxins Hp II, Hp III, and toxin I fromStichodactyla helianthus (Sh I). The similarity in deviations in chemical shift as a function of sequence position for these four toxins emphasizes the overall structural homology among these polypeptides. Norton, Raymond S. aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 12(1993), 3 vom: 01. Juni, Seite 371-378 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:12 year:1993 number:3 day:01 month:06 pages:371-378 https://dx.doi.org/10.1007/BF01028199 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 12 1993 3 01 06 371-378 |
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10.1007/BF01028199 doi (DE-627)SPR052838730 (SPR)BF01028199-e DE-627 ger DE-627 rakwb eng Hinds, Mark G. verfasserin aut $ Sequential^{1} $H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins 1993 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1993 Abstract The complete sequence-specific assignment of resonances in $ the^{1} $H-NMR spectrum of the polypeptide neurotoxin III (Hm III) from the sea anemoneHeteractis macrodactylus is described. Comparison of the chemical shifts and pattern of NOEs for Hm III with those for the related toxin Hp III fromHeteractis paumotensis, which differs only in the substitution of Asn for Tyr at position 11, shows that the overall secondary and tertiary structures are conserved. The largest differences in chemical shift caused by the substitution at position 11 are observed for the NH resonances of Arg-13, Thr-14, Ala-15, Leu-17, and Cys-26. The $ C^{α} $H resonances influenced most are those of ASP-6, Gly-9, Leu-17, and Glu-42, while the most affected $ C^{β} $H resonances are from Leu-17, Glu-28, and Lys-32. The absence of long-range NOEs to the aromatic ring of Tyr-11 as well as the lack of significant chemical shift effects on residues outside the loop comprising residues 7–16 confirm that this part of the loop makes no long-lived contacts with the rest of the molecule. The deviations from random coil shifts of Hm III are compared with those of the related anemone toxins Hp II, Hp III, and toxin I fromStichodactyla helianthus (Sh I). The similarity in deviations in chemical shift as a function of sequence position for these four toxins emphasizes the overall structural homology among these polypeptides. Norton, Raymond S. aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 12(1993), 3 vom: 01. Juni, Seite 371-378 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:12 year:1993 number:3 day:01 month:06 pages:371-378 https://dx.doi.org/10.1007/BF01028199 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 12 1993 3 01 06 371-378 |
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$ sequential^{1} $h-nmr assignments of neurotoxin iii from the sea anemoneheteractis macrodactylus and structural comparison with related toxins |
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$ Sequential^{1} $H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins |
| abstract |
Abstract The complete sequence-specific assignment of resonances in $ the^{1} $H-NMR spectrum of the polypeptide neurotoxin III (Hm III) from the sea anemoneHeteractis macrodactylus is described. Comparison of the chemical shifts and pattern of NOEs for Hm III with those for the related toxin Hp III fromHeteractis paumotensis, which differs only in the substitution of Asn for Tyr at position 11, shows that the overall secondary and tertiary structures are conserved. The largest differences in chemical shift caused by the substitution at position 11 are observed for the NH resonances of Arg-13, Thr-14, Ala-15, Leu-17, and Cys-26. The $ C^{α} $H resonances influenced most are those of ASP-6, Gly-9, Leu-17, and Glu-42, while the most affected $ C^{β} $H resonances are from Leu-17, Glu-28, and Lys-32. The absence of long-range NOEs to the aromatic ring of Tyr-11 as well as the lack of significant chemical shift effects on residues outside the loop comprising residues 7–16 confirm that this part of the loop makes no long-lived contacts with the rest of the molecule. The deviations from random coil shifts of Hm III are compared with those of the related anemone toxins Hp II, Hp III, and toxin I fromStichodactyla helianthus (Sh I). The similarity in deviations in chemical shift as a function of sequence position for these four toxins emphasizes the overall structural homology among these polypeptides. © Plenum Publishing Corporation 1993 |
| abstractGer |
Abstract The complete sequence-specific assignment of resonances in $ the^{1} $H-NMR spectrum of the polypeptide neurotoxin III (Hm III) from the sea anemoneHeteractis macrodactylus is described. Comparison of the chemical shifts and pattern of NOEs for Hm III with those for the related toxin Hp III fromHeteractis paumotensis, which differs only in the substitution of Asn for Tyr at position 11, shows that the overall secondary and tertiary structures are conserved. The largest differences in chemical shift caused by the substitution at position 11 are observed for the NH resonances of Arg-13, Thr-14, Ala-15, Leu-17, and Cys-26. The $ C^{α} $H resonances influenced most are those of ASP-6, Gly-9, Leu-17, and Glu-42, while the most affected $ C^{β} $H resonances are from Leu-17, Glu-28, and Lys-32. The absence of long-range NOEs to the aromatic ring of Tyr-11 as well as the lack of significant chemical shift effects on residues outside the loop comprising residues 7–16 confirm that this part of the loop makes no long-lived contacts with the rest of the molecule. The deviations from random coil shifts of Hm III are compared with those of the related anemone toxins Hp II, Hp III, and toxin I fromStichodactyla helianthus (Sh I). The similarity in deviations in chemical shift as a function of sequence position for these four toxins emphasizes the overall structural homology among these polypeptides. © Plenum Publishing Corporation 1993 |
| abstract_unstemmed |
Abstract The complete sequence-specific assignment of resonances in $ the^{1} $H-NMR spectrum of the polypeptide neurotoxin III (Hm III) from the sea anemoneHeteractis macrodactylus is described. Comparison of the chemical shifts and pattern of NOEs for Hm III with those for the related toxin Hp III fromHeteractis paumotensis, which differs only in the substitution of Asn for Tyr at position 11, shows that the overall secondary and tertiary structures are conserved. The largest differences in chemical shift caused by the substitution at position 11 are observed for the NH resonances of Arg-13, Thr-14, Ala-15, Leu-17, and Cys-26. The $ C^{α} $H resonances influenced most are those of ASP-6, Gly-9, Leu-17, and Glu-42, while the most affected $ C^{β} $H resonances are from Leu-17, Glu-28, and Lys-32. The absence of long-range NOEs to the aromatic ring of Tyr-11 as well as the lack of significant chemical shift effects on residues outside the loop comprising residues 7–16 confirm that this part of the loop makes no long-lived contacts with the rest of the molecule. The deviations from random coil shifts of Hm III are compared with those of the related anemone toxins Hp II, Hp III, and toxin I fromStichodactyla helianthus (Sh I). The similarity in deviations in chemical shift as a function of sequence position for these four toxins emphasizes the overall structural homology among these polypeptides. © Plenum Publishing Corporation 1993 |
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| title_short |
$ Sequential^{1} $H-NMR assignments of neurotoxin III from the sea anemoneHeteractis macrodactylus and structural comparison with related toxins |
| url |
https://dx.doi.org/10.1007/BF01028199 |
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| author2 |
Norton, Raymond S. |
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| doi_str |
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| up_date |
2024-07-03T15:08:42.067Z |
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