Structure and conformation of peptides involving prolyl residue III. L-Prolyl-L-isoleucine monohydrate
The dipeptide, L‐prolyl‐L‐isoleucine monohydrate (C11 H20N2O3· H2O, molecular weight 246.3) crystallizes in the monoclinic space group P21, with a = 6.601(3)Å, b = 5.413(3) Å, c = 19.128(6) Å, β= 98.1(1)°, Z = 2, Do = 1.20g·cm‐3 and Dc = 1.208g·cm‐3. The structure was solved by MULTAN–80 and refined...
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| Veröffentlicht in: | International Journal of Peptide and Protein Research 1989-03, Vol.33 (3), p.191-194 |
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| container_title | International Journal of Peptide and Protein Research |
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| creator | PANNEERSELVAM, K. CHACKO, K.K. VEENA, R. |
| description | The dipeptide, L‐prolyl‐L‐isoleucine monohydrate (C11 H20N2O3· H2O, molecular weight 246.3) crystallizes in the monoclinic space group P21, with a = 6.601(3)Å, b = 5.413(3) Å, c = 19.128(6) Å, β= 98.1(1)°, Z = 2, Do = 1.20g·cm‐3 and Dc = 1.208g·cm‐3. The structure was solved by MULTAN–80 and refined to a final R‐factor of 0.081 for 594 reflections measured on a Enraf Nonius CAD‐4 diffractometer. The peptide linkage exists in the trans conformation. The pyrrolidine ring is disordered with two alternate envelope conformations for the Cγ atom. The values of the sidechain torsion angles are: χ11=– 63.6(17)°, χ12= 171.1(16)° and χ2=– 59.6(21)° for isoleucine (C‐terminal). The crystal structure is stabilized by a three‐dimensional network of N—H ⋯ O, O—H ⋯ O and C—H ⋯ O hydrogen bonds. The dipeptide exists in the extended Conformation. |
| doi_str_mv | 10.1111/j.1399-3011.1989.tb00208.x |
| format | Article |
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L-Prolyl-L-isoleucine monohydrate</title><source>Wiley Journals</source><creator>PANNEERSELVAM, K. ; CHACKO, K.K. ; VEENA, R.</creator><creatorcontrib>PANNEERSELVAM, K. ; CHACKO, K.K. ; VEENA, R.</creatorcontrib><description>The dipeptide, L‐prolyl‐L‐isoleucine monohydrate (C11 H20N2O3· H2O, molecular weight 246.3) crystallizes in the monoclinic space group P21, with a = 6.601(3)Å, b = 5.413(3) Å, c = 19.128(6) Å, β= 98.1(1)°, Z = 2, Do = 1.20g·cm‐3 and Dc = 1.208g·cm‐3. The structure was solved by MULTAN–80 and refined to a final R‐factor of 0.081 for 594 reflections measured on a Enraf Nonius CAD‐4 diffractometer. The peptide linkage exists in the trans conformation. The pyrrolidine ring is disordered with two alternate envelope conformations for the Cγ atom. The values of the sidechain torsion angles are: χ11=– 63.6(17)°, χ12= 171.1(16)° and χ2=– 59.6(21)° for isoleucine (C‐terminal). The crystal structure is stabilized by a three‐dimensional network of N—H ⋯ O, O—H ⋯ O and C—H ⋯ O hydrogen bonds. The dipeptide exists in the extended Conformation.</description><identifier>ISSN: 0367-8377</identifier><identifier>EISSN: 1399-3011</identifier><identifier>DOI: 10.1111/j.1399-3011.1989.tb00208.x</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>conformation ; crystal structure ; dipeptide ; L-prolyl-L-isoleucine ; X-ray structure</subject><ispartof>International Journal of Peptide and Protein Research, 1989-03, Vol.33 (3), p.191-194</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3031-d74e29841bbcb8198bd38020aaf6ad67de90233963e7190ff1acce63c2eb24e3</citedby><cites>FETCH-LOGICAL-c3031-d74e29841bbcb8198bd38020aaf6ad67de90233963e7190ff1acce63c2eb24e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1399-3011.1989.tb00208.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1399-3011.1989.tb00208.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids></links><search><creatorcontrib>PANNEERSELVAM, K.</creatorcontrib><creatorcontrib>CHACKO, K.K.</creatorcontrib><creatorcontrib>VEENA, R.</creatorcontrib><title>Structure and conformation of peptides involving prolyl residue III. L-Prolyl-L-isoleucine monohydrate</title><title>International Journal of Peptide and Protein Research</title><description>The dipeptide, L‐prolyl‐L‐isoleucine monohydrate (C11 H20N2O3· H2O, molecular weight 246.3) crystallizes in the monoclinic space group P21, with a = 6.601(3)Å, b = 5.413(3) Å, c = 19.128(6) Å, β= 98.1(1)°, Z = 2, Do = 1.20g·cm‐3 and Dc = 1.208g·cm‐3. The structure was solved by MULTAN–80 and refined to a final R‐factor of 0.081 for 594 reflections measured on a Enraf Nonius CAD‐4 diffractometer. The peptide linkage exists in the trans conformation. The pyrrolidine ring is disordered with two alternate envelope conformations for the Cγ atom. The values of the sidechain torsion angles are: χ11=– 63.6(17)°, χ12= 171.1(16)° and χ2=– 59.6(21)° for isoleucine (C‐terminal). The crystal structure is stabilized by a three‐dimensional network of N—H ⋯ O, O—H ⋯ O and C—H ⋯ O hydrogen bonds. The dipeptide exists in the extended Conformation.</description><subject>conformation</subject><subject>crystal structure</subject><subject>dipeptide</subject><subject>L-prolyl-L-isoleucine</subject><subject>X-ray structure</subject><issn>0367-8377</issn><issn>1399-3011</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><recordid>eNqVkE1P4zAQhi0EEuXjP1gc9uasnSlxvBcEZVsqRSwrkDhajjNh3U3jYifQ_nuSLeK-cxlpZt53Zh5CLgRPxBDfV4kApRhwIRKhcpV0Jecpz5PtAZl8tQ7JhEMmWQ5SHpOTGFecwxRkOiH1Yxd62_UBqWkran1b-7A2nfMt9TXd4KZzFUbq2jffvLn2hW6Cb3YNDRhd1SNdLpcJLdjDvyormIu-wd66Funat_7PrgqmwzNyVJsm4vlnPiVP859PsztW_FosZ9cFs8BBsEpOMVX5VJSlLfPhobKCfPjHmDozVSYrVDwFUBmgFIrXtTDWYgY2xTKdIpySb3vb4cjXHmOn1y5abBrTou-jFpephBzEMPhjP2iDjzFgrTfBrU3YacH1SFav9IhPj_j0SFZ_ktXbQXy1F7-7Bnf_odSzm9tbocb1bO_gYofbLwcT_upMgrzUz_cL_bx4-D2_m9_rAj4AvOiSTA</recordid><startdate>198903</startdate><enddate>198903</enddate><creator>PANNEERSELVAM, K.</creator><creator>CHACKO, K.K.</creator><creator>VEENA, R.</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>198903</creationdate><title>Structure and conformation of peptides involving prolyl residue III. L-Prolyl-L-isoleucine monohydrate</title><author>PANNEERSELVAM, K. ; CHACKO, K.K. ; VEENA, R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3031-d74e29841bbcb8198bd38020aaf6ad67de90233963e7190ff1acce63c2eb24e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>conformation</topic><topic>crystal structure</topic><topic>dipeptide</topic><topic>L-prolyl-L-isoleucine</topic><topic>X-ray structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>PANNEERSELVAM, K.</creatorcontrib><creatorcontrib>CHACKO, K.K.</creatorcontrib><creatorcontrib>VEENA, R.</creatorcontrib><collection>Istex</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>International Journal of Peptide and Protein Research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>PANNEERSELVAM, K.</au><au>CHACKO, K.K.</au><au>VEENA, R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure and conformation of peptides involving prolyl residue III. L-Prolyl-L-isoleucine monohydrate</atitle><jtitle>International Journal of Peptide and Protein Research</jtitle><date>1989-03</date><risdate>1989</risdate><volume>33</volume><issue>3</issue><spage>191</spage><epage>194</epage><pages>191-194</pages><issn>0367-8377</issn><eissn>1399-3011</eissn><abstract>The dipeptide, L‐prolyl‐L‐isoleucine monohydrate (C11 H20N2O3· H2O, molecular weight 246.3) crystallizes in the monoclinic space group P21, with a = 6.601(3)Å, b = 5.413(3) Å, c = 19.128(6) Å, β= 98.1(1)°, Z = 2, Do = 1.20g·cm‐3 and Dc = 1.208g·cm‐3. The structure was solved by MULTAN–80 and refined to a final R‐factor of 0.081 for 594 reflections measured on a Enraf Nonius CAD‐4 diffractometer. The peptide linkage exists in the trans conformation. The pyrrolidine ring is disordered with two alternate envelope conformations for the Cγ atom. The values of the sidechain torsion angles are: χ11=– 63.6(17)°, χ12= 171.1(16)° and χ2=– 59.6(21)° for isoleucine (C‐terminal). The crystal structure is stabilized by a three‐dimensional network of N—H ⋯ O, O—H ⋯ O and C—H ⋯ O hydrogen bonds. The dipeptide exists in the extended Conformation.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1111/j.1399-3011.1989.tb00208.x</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0367-8377 |
| ispartof | International Journal of Peptide and Protein Research, 1989-03, Vol.33 (3), p.191-194 |
| issn | 0367-8377 1399-3011 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15273831 |
| source | Wiley Journals |
| subjects | conformation crystal structure dipeptide L-prolyl-L-isoleucine X-ray structure |
| title | Structure and conformation of peptides involving prolyl residue III. L-Prolyl-L-isoleucine monohydrate |
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