Conformation of gramicidin S
A molecular conformation of Gramicidin S was derived on the basis of conformational calculations taking into account the available experimental data. The conformation is characterized by a dyad axis which relates the two chemically equivalent halves of the molecule and contains four hydrogen bonds;...
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Veröffentlicht in: | Biopolymers 1971-01, Vol.10 (4), p.699-710 |
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creator | De Santis, P. Liquori, A. M. |
description | A molecular conformation of Gramicidin S was derived on the basis of conformational calculations taking into account the available experimental data.
The conformation is characterized by a dyad axis which relates the two chemically equivalent halves of the molecule and contains four hydrogen bonds; other structural features agree with experimental results. X Ray Crystallographic evidences for the relative position of the Ornithine residues is also reported which supports an important feature of the structure of Gramicidin S. |
doi_str_mv | 10.1002/bip.360100408 |
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The conformation is characterized by a dyad axis which relates the two chemically equivalent halves of the molecule and contains four hydrogen bonds; other structural features agree with experimental results. X Ray Crystallographic evidences for the relative position of the Ornithine residues is also reported which supports an important feature of the structure of Gramicidin S.</description><identifier>ISSN: 0006-3525</identifier><identifier>EISSN: 1097-0282</identifier><identifier>DOI: 10.1002/bip.360100408</identifier><identifier>PMID: 5552139</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Molecular Biology ; Peptides ; Peptides, Cyclic ; Tyrothricin ; X-Ray Diffraction</subject><ispartof>Biopolymers, 1971-01, Vol.10 (4), p.699-710</ispartof><rights>Copyright © 1971 John Wiley & Sons, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3748-3c8678bf8099a95a917741cf81c9d1fcf9eff589504a297750a19df2b0d3001f3</citedby><cites>FETCH-LOGICAL-c3748-3c8678bf8099a95a917741cf81c9d1fcf9eff589504a297750a19df2b0d3001f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbip.360100408$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbip.360100408$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5552139$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>De Santis, P.</creatorcontrib><creatorcontrib>Liquori, A. M.</creatorcontrib><title>Conformation of gramicidin S</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>A molecular conformation of Gramicidin S was derived on the basis of conformational calculations taking into account the available experimental data.
The conformation is characterized by a dyad axis which relates the two chemically equivalent halves of the molecule and contains four hydrogen bonds; other structural features agree with experimental results. X Ray Crystallographic evidences for the relative position of the Ornithine residues is also reported which supports an important feature of the structure of Gramicidin S.</description><subject>Molecular Biology</subject><subject>Peptides</subject><subject>Peptides, Cyclic</subject><subject>Tyrothricin</subject><subject>X-Ray Diffraction</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1971</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1PAjEQhhujQUSP3jTh5G1xut1u26MQRZCoRA3HptttTXU_oIUo_941bIgnTzPJPPNk5kXoHMMAA8TXmVsOSApNnwA_QF0MgkUQ8_gQdQEgjQiN6TE6CeGjQRKCoYM6lNIYE9FFF6O6srUv1drVVb-2_XevSqdd7qr-yyk6sqoI5qytPfR2d_s6uo9mT-PJ6GYWacISHhHNU8Yzy0EIJagSmLEEa8uxFjm22gpjLeWCQqJiwRgFhUVu4wxyAoAt6aGrnXfp69XGhLUsXdCmKFRl6k2QjThhNMUNGO1A7esQvLFy6V2p_FZikL9pyCYNuU-j4S9b8SYrTb6n2_ebOdvNv1xhtv_L5HDy_NfcXuLC2nzvN5X_lCkjjMrF41iO5zBczKdT-UB-AMsyd10</recordid><startdate>19710101</startdate><enddate>19710101</enddate><creator>De Santis, P.</creator><creator>Liquori, A. M.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</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>19710101</creationdate><title>Conformation of gramicidin S</title><author>De Santis, P. ; Liquori, A. M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3748-3c8678bf8099a95a917741cf81c9d1fcf9eff589504a297750a19df2b0d3001f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1971</creationdate><topic>Molecular Biology</topic><topic>Peptides</topic><topic>Peptides, Cyclic</topic><topic>Tyrothricin</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>De Santis, P.</creatorcontrib><creatorcontrib>Liquori, A. M.</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>Biopolymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>De Santis, P.</au><au>Liquori, A. M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conformation of gramicidin S</atitle><jtitle>Biopolymers</jtitle><addtitle>Biopolymers</addtitle><date>1971-01-01</date><risdate>1971</risdate><volume>10</volume><issue>4</issue><spage>699</spage><epage>710</epage><pages>699-710</pages><issn>0006-3525</issn><eissn>1097-0282</eissn><abstract>A molecular conformation of Gramicidin S was derived on the basis of conformational calculations taking into account the available experimental data.
The conformation is characterized by a dyad axis which relates the two chemically equivalent halves of the molecule and contains four hydrogen bonds; other structural features agree with experimental results. X Ray Crystallographic evidences for the relative position of the Ornithine residues is also reported which supports an important feature of the structure of Gramicidin S.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>5552139</pmid><doi>10.1002/bip.360100408</doi><tpages>12</tpages></addata></record> |
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subjects | Molecular Biology Peptides Peptides, Cyclic Tyrothricin X-Ray Diffraction |
title | Conformation of gramicidin S |
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