A THEORETICAL STUDY OF THE STRUCTURES OF (GLY-PRO-LEU)n AND (GLY-LEU-PRO)n
Theoretical conformation studies have been carried out for the polytripeptides (Gly‐Pro‐Leu)n and (Gly‐Leu‐Pro)n and the Fourier transforms of the structures have been calculated. X‐ray powder patterns of these polymers had indicated that both these polymers take up coiled‐coil triple‐helical struct...
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| Veröffentlicht in: | International Journal of Peptide and Protein Research 1978-01, Vol.11 (1), p.73-81 |
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| container_title | International Journal of Peptide and Protein Research |
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| creator | Bansal, M. Ramachandran, G.N. |
| description | Theoretical conformation studies have been carried out for the polytripeptides (Gly‐Pro‐Leu)n and (Gly‐Leu‐Pro)n and the Fourier transforms of the structures have been calculated. X‐ray powder patterns of these polymers had indicated that both these polymers take up coiled‐coil triple‐helical structures, but in the case of (Gly‐Pro‐Leu)n it was not clear whether the triple helix is formed by three parallel polypeptide chains or by a single chain folding back on itself (Scatturin et al 1975). Our studies show that both the polytripeptides can take up stereochemically satisfactory triple‐helical structures with three parallel chains. There is also very good agreement between the calculated intensity distribution and that of the observed X‐ray pattern, in each case. |
| doi_str_mv | 10.1111/j.1399-3011.1978.tb02823.x |
| format | Article |
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X‐ray powder patterns of these polymers had indicated that both these polymers take up coiled‐coil triple‐helical structures, but in the case of (Gly‐Pro‐Leu)n it was not clear whether the triple helix is formed by three parallel polypeptide chains or by a single chain folding back on itself (Scatturin et al 1975). Our studies show that both the polytripeptides can take up stereochemically satisfactory triple‐helical structures with three parallel chains. There is also very good agreement between the calculated intensity distribution and that of the observed X‐ray pattern, in each case.</description><identifier>ISSN: 0367-8377</identifier><identifier>EISSN: 1399-3011</identifier><identifier>DOI: 10.1111/j.1399-3011.1978.tb02823.x</identifier><identifier>PMID: 631989</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>(Gly-Leu-Pro)n ; (Gly-Pro-Leu)n ; Amino Acid Sequence ; Models, Chemical ; Models, Structural ; Molecular Conformation ; Peptides ; polytripeptide models for collagen ; theoretical conformation studies ; X-Ray Diffraction</subject><ispartof>International Journal of Peptide and Protein Research, 1978-01, Vol.11 (1), p.73-81</ispartof><rights>1978 Munksgaard International Publishers Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4063-d22ec2c17d78f7405238f3e3793dcbbca416e975d0832a7d4f4601553b1d888a3</citedby><cites>FETCH-LOGICAL-c4063-d22ec2c17d78f7405238f3e3793dcbbca416e975d0832a7d4f4601553b1d888a3</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.1399-3011.1978.tb02823.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1399-3011.1978.tb02823.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/631989$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bansal, M.</creatorcontrib><creatorcontrib>Ramachandran, G.N.</creatorcontrib><title>A THEORETICAL STUDY OF THE STRUCTURES OF (GLY-PRO-LEU)n AND (GLY-LEU-PRO)n</title><title>International Journal of Peptide and Protein Research</title><addtitle>Int J Pept Protein Res</addtitle><description>Theoretical conformation studies have been carried out for the polytripeptides (Gly‐Pro‐Leu)n and (Gly‐Leu‐Pro)n and the Fourier transforms of the structures have been calculated. X‐ray powder patterns of these polymers had indicated that both these polymers take up coiled‐coil triple‐helical structures, but in the case of (Gly‐Pro‐Leu)n it was not clear whether the triple helix is formed by three parallel polypeptide chains or by a single chain folding back on itself (Scatturin et al 1975). Our studies show that both the polytripeptides can take up stereochemically satisfactory triple‐helical structures with three parallel chains. There is also very good agreement between the calculated intensity distribution and that of the observed X‐ray pattern, in each case.</description><subject>(Gly-Leu-Pro)n</subject><subject>(Gly-Pro-Leu)n</subject><subject>Amino Acid Sequence</subject><subject>Models, Chemical</subject><subject>Models, Structural</subject><subject>Molecular Conformation</subject><subject>Peptides</subject><subject>polytripeptide models for collagen</subject><subject>theoretical conformation studies</subject><subject>X-Ray Diffraction</subject><issn>0367-8377</issn><issn>1399-3011</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkE1PwkAQhjfGL0T_gQfiwcihdXen7e56MIG2gIaAKW2Mp00_tglYPuxChH9vmxLu7mUz78w8kzwIPRBskuo9L0wCQhiACTGJYNzcJphyCub-DLVOrXPUwuAwgwNj1-hG6wXGYAGjV-jSASK4aKH3Xicc-dPAD9_c3rgzCyPvqzMd1GFVBJEbRoE_q5On4fjL-AimxtiPuqtOb-I1UVXWcXd1iy7yuNDq7vi3UTTwQ3dkjKfDGm6kFnbAyChVKU0JyxjPmYVtCjwHBUxAliZJGlvEUYLZGeZAY5ZZueVgYtuQkIxzHkMbPTbcTbn-2Sm9lcu5TlVRxCu13mnJgVMmCKsGX5rBtFxrXapcbsr5Mi4PkmBZe5QLWcuStSxZe5RHj3JfLd8fr-ySpcpOq424qv3atH_nhTr8AyzdvucxqABGA5jrrdqfAHH5LR0GzJafk6G0qHAGgefKPvwBDpGJVw</recordid><startdate>197801</startdate><enddate>197801</enddate><creator>Bansal, M.</creator><creator>Ramachandran, G.N.</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>197801</creationdate><title>A THEORETICAL STUDY OF THE STRUCTURES OF (GLY-PRO-LEU)n AND (GLY-LEU-PRO)n</title><author>Bansal, M. ; Ramachandran, G.N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4063-d22ec2c17d78f7405238f3e3793dcbbca416e975d0832a7d4f4601553b1d888a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>(Gly-Leu-Pro)n</topic><topic>(Gly-Pro-Leu)n</topic><topic>Amino Acid Sequence</topic><topic>Models, Chemical</topic><topic>Models, Structural</topic><topic>Molecular Conformation</topic><topic>Peptides</topic><topic>polytripeptide models for collagen</topic><topic>theoretical conformation studies</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bansal, M.</creatorcontrib><creatorcontrib>Ramachandran, G.N.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>International Journal of Peptide and Protein Research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bansal, M.</au><au>Ramachandran, G.N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A THEORETICAL STUDY OF THE STRUCTURES OF (GLY-PRO-LEU)n AND (GLY-LEU-PRO)n</atitle><jtitle>International Journal of Peptide and Protein Research</jtitle><addtitle>Int J Pept Protein Res</addtitle><date>1978-01</date><risdate>1978</risdate><volume>11</volume><issue>1</issue><spage>73</spage><epage>81</epage><pages>73-81</pages><issn>0367-8377</issn><eissn>1399-3011</eissn><abstract>Theoretical conformation studies have been carried out for the polytripeptides (Gly‐Pro‐Leu)n and (Gly‐Leu‐Pro)n and the Fourier transforms of the structures have been calculated. X‐ray powder patterns of these polymers had indicated that both these polymers take up coiled‐coil triple‐helical structures, but in the case of (Gly‐Pro‐Leu)n it was not clear whether the triple helix is formed by three parallel polypeptide chains or by a single chain folding back on itself (Scatturin et al 1975). Our studies show that both the polytripeptides can take up stereochemically satisfactory triple‐helical structures with three parallel chains. There is also very good agreement between the calculated intensity distribution and that of the observed X‐ray pattern, in each case.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>631989</pmid><doi>10.1111/j.1399-3011.1978.tb02823.x</doi><tpages>9</tpages></addata></record> |
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| identifier | ISSN: 0367-8377 |
| ispartof | International Journal of Peptide and Protein Research, 1978-01, Vol.11 (1), p.73-81 |
| issn | 0367-8377 1399-3011 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | (Gly-Leu-Pro)n (Gly-Pro-Leu)n Amino Acid Sequence Models, Chemical Models, Structural Molecular Conformation Peptides polytripeptide models for collagen theoretical conformation studies X-Ray Diffraction |
| title | A THEORETICAL STUDY OF THE STRUCTURES OF (GLY-PRO-LEU)n AND (GLY-LEU-PRO)n |
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