Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density
Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-facto...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Matsumoto, Osamu [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1990 |
|---|
| Anmerkung: |
© Plenum Publishing Corporation 1990 |
|---|
| Übergeordnetes Werk: |
Enthalten in: The protein journal - Dordrecht : Springer Science + Business Media B.V., 2004, 9(1990), 5 vom: 01. Okt., Seite 589-593 |
|---|---|
| Übergeordnetes Werk: |
volume:9 ; year:1990 ; number:5 ; day:01 ; month:10 ; pages:589-593 |
| Links: |
|---|
| DOI / URN: |
10.1007/BF01025012 |
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| 245 | 1 | 0 | |a Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density |
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| 520 | |a Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin. | ||
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10.1007/BF01025012 doi (DE-627)SPR052788326 (SPR)BF01025012-e DE-627 ger DE-627 rakwb eng Matsumoto, Osamu verfasserin aut Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density 1990 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1990 Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin. Taga, Tooru aut Higashi, Tsuneyuki aut Matsushima, Masaaki aut Machida, Katsunosuke aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 9(1990), 5 vom: 01. Okt., Seite 589-593 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:9 year:1990 number:5 day:01 month:10 pages:589-593 https://dx.doi.org/10.1007/BF01025012 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 9 1990 5 01 10 589-593 |
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10.1007/BF01025012 doi (DE-627)SPR052788326 (SPR)BF01025012-e DE-627 ger DE-627 rakwb eng Matsumoto, Osamu verfasserin aut Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density 1990 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1990 Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin. Taga, Tooru aut Higashi, Tsuneyuki aut Matsushima, Masaaki aut Machida, Katsunosuke aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 9(1990), 5 vom: 01. Okt., Seite 589-593 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:9 year:1990 number:5 day:01 month:10 pages:589-593 https://dx.doi.org/10.1007/BF01025012 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 9 1990 5 01 10 589-593 |
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10.1007/BF01025012 doi (DE-627)SPR052788326 (SPR)BF01025012-e DE-627 ger DE-627 rakwb eng Matsumoto, Osamu verfasserin aut Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density 1990 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1990 Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin. Taga, Tooru aut Higashi, Tsuneyuki aut Matsushima, Masaaki aut Machida, Katsunosuke aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 9(1990), 5 vom: 01. Okt., Seite 589-593 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:9 year:1990 number:5 day:01 month:10 pages:589-593 https://dx.doi.org/10.1007/BF01025012 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 9 1990 5 01 10 589-593 |
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10.1007/BF01025012 doi (DE-627)SPR052788326 (SPR)BF01025012-e DE-627 ger DE-627 rakwb eng Matsumoto, Osamu verfasserin aut Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density 1990 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1990 Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin. Taga, Tooru aut Higashi, Tsuneyuki aut Matsushima, Masaaki aut Machida, Katsunosuke aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 9(1990), 5 vom: 01. Okt., Seite 589-593 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:9 year:1990 number:5 day:01 month:10 pages:589-593 https://dx.doi.org/10.1007/BF01025012 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 9 1990 5 01 10 589-593 |
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10.1007/BF01025012 doi (DE-627)SPR052788326 (SPR)BF01025012-e DE-627 ger DE-627 rakwb eng Matsumoto, Osamu verfasserin aut Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density 1990 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1990 Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin. Taga, Tooru aut Higashi, Tsuneyuki aut Matsushima, Masaaki aut Machida, Katsunosuke aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 9(1990), 5 vom: 01. Okt., Seite 589-593 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:9 year:1990 number:5 day:01 month:10 pages:589-593 https://dx.doi.org/10.1007/BF01025012 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 9 1990 5 01 10 589-593 |
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Matsumoto, Osamu |
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Matsumoto, Osamu Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density |
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Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density |
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Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density |
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Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin. © Plenum Publishing Corporation 1990 |
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Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin. © Plenum Publishing Corporation 1990 |
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Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin. © Plenum Publishing Corporation 1990 |
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Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR052788326</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230819064754.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">230819s1990 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/BF01025012</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR052788326</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)BF01025012-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Matsumoto, Osamu</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-$ NH_{2} $): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1990</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Plenum Publishing Corporation 1990</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract The title tetrapeptide, Leu-Arg-Pro-Gly-$ NH_{2} $, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. 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