Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A
The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], show...
Ausführliche Beschreibung
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1995 |
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| Umfang: |
3 Ill. ; 4 Tab. 8 |
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| Reproduktion: |
Wiley InterScience Backfile Collection 1832-2000 |
|---|---|
| Übergeordnetes Werk: |
in: Biopolymers - New York : John Wiley & Sons, Inc., 36(1995) vom: Apr., Seite 453-460 |
| Übergeordnetes Werk: |
volume:36 ; year:1995 ; month:04 ; pages:453-460 ; extent:8 |
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| 520 | |a The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. | ||
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(DE-627)NLEJ159592178 DE-627 ger DE-627 rakwb eng Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A 1995 3 Ill. 4 Tab. 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. Wiley InterScience Backfile Collection 1832-2000 Saviano, Michele oth Rossi, Filomena oth Filizola, Marta oth Isernia, Carla oth Di Blasio, Benedetto oth Benedetti, Ettore oth Pedone, Carlo oth Siemion, Ignacy Z. oth Pedyczak, Artur oth in Biopolymers New York : John Wiley & Sons, Inc. 36(1995) vom: Apr., Seite 453-460 (DE-627)NLEJ15907066X (DE-600)1480801-8 0006-3525 nnns volume:36 year:1995 month:04 pages:453-460 extent:8 http://dx.doi.org/10.1002/bip.360360408 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 36 1995 4 453-460 8 |
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(DE-627)NLEJ159592178 DE-627 ger DE-627 rakwb eng Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A 1995 3 Ill. 4 Tab. 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. Wiley InterScience Backfile Collection 1832-2000 Saviano, Michele oth Rossi, Filomena oth Filizola, Marta oth Isernia, Carla oth Di Blasio, Benedetto oth Benedetti, Ettore oth Pedone, Carlo oth Siemion, Ignacy Z. oth Pedyczak, Artur oth in Biopolymers New York : John Wiley & Sons, Inc. 36(1995) vom: Apr., Seite 453-460 (DE-627)NLEJ15907066X (DE-600)1480801-8 0006-3525 nnns volume:36 year:1995 month:04 pages:453-460 extent:8 http://dx.doi.org/10.1002/bip.360360408 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 36 1995 4 453-460 8 |
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(DE-627)NLEJ159592178 DE-627 ger DE-627 rakwb eng Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A 1995 3 Ill. 4 Tab. 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. Wiley InterScience Backfile Collection 1832-2000 Saviano, Michele oth Rossi, Filomena oth Filizola, Marta oth Isernia, Carla oth Di Blasio, Benedetto oth Benedetti, Ettore oth Pedone, Carlo oth Siemion, Ignacy Z. oth Pedyczak, Artur oth in Biopolymers New York : John Wiley & Sons, Inc. 36(1995) vom: Apr., Seite 453-460 (DE-627)NLEJ15907066X (DE-600)1480801-8 0006-3525 nnns volume:36 year:1995 month:04 pages:453-460 extent:8 http://dx.doi.org/10.1002/bip.360360408 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 36 1995 4 453-460 8 |
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(DE-627)NLEJ159592178 DE-627 ger DE-627 rakwb eng Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A 1995 3 Ill. 4 Tab. 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. Wiley InterScience Backfile Collection 1832-2000 Saviano, Michele oth Rossi, Filomena oth Filizola, Marta oth Isernia, Carla oth Di Blasio, Benedetto oth Benedetti, Ettore oth Pedone, Carlo oth Siemion, Ignacy Z. oth Pedyczak, Artur oth in Biopolymers New York : John Wiley & Sons, Inc. 36(1995) vom: Apr., Seite 453-460 (DE-627)NLEJ15907066X (DE-600)1480801-8 0006-3525 nnns volume:36 year:1995 month:04 pages:453-460 extent:8 http://dx.doi.org/10.1002/bip.360360408 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 36 1995 4 453-460 8 |
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(DE-627)NLEJ159592178 DE-627 ger DE-627 rakwb eng Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A 1995 3 Ill. 4 Tab. 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. Wiley InterScience Backfile Collection 1832-2000 Saviano, Michele oth Rossi, Filomena oth Filizola, Marta oth Isernia, Carla oth Di Blasio, Benedetto oth Benedetti, Ettore oth Pedone, Carlo oth Siemion, Ignacy Z. oth Pedyczak, Artur oth in Biopolymers New York : John Wiley & Sons, Inc. 36(1995) vom: Apr., Seite 453-460 (DE-627)NLEJ15907066X (DE-600)1480801-8 0006-3525 nnns volume:36 year:1995 month:04 pages:453-460 extent:8 http://dx.doi.org/10.1002/bip.360360408 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 36 1995 4 453-460 8 |
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Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A |
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The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. |
| abstractGer |
The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. |
| abstract_unstemmed |
The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ159592178</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707012515.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070201s1995 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ159592178</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1995</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="b">3 Ill.</subfield><subfield code="b">4 Tab.</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">8</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N-H- O=C hydrogen bonds, with formation of one C17 ring structure, one α-turn (C13), one inverse γ-turn (C7), and two β-turns (C10, one of type III and one of type 1). The Pro1-Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. 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