Carbon-13 Fourier transform nuclear magnetic resonance studies of peptides
The carbon-13 nuclear magnetic resonance (CMR) spectra of several small peptides have been obtained at 25.1 MHz and natural abundance of 13C using the Fourier transform technique with proton noise decoupling. Chemical shift values have been studied as a function of pH. The peptide corresponding to t...
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Veröffentlicht in: | Biochemical and biophysical research communications 1971-03, Vol.42 (6), p.1148-1155 |
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container_title | Biochemical and biophysical research communications |
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creator | Freedman, Murray H. Cohen, Jack S. Chaiken, Irwin M. |
description | The carbon-13 nuclear magnetic resonance (CMR) spectra of several small peptides have been obtained at 25.1 MHz and natural abundance of
13C using the Fourier transform technique with proton noise decoupling. Chemical shift values have been studied as a function of pH. The peptide corresponding to the 1–15 sequence of ribonuclease has been synthesized both with normal and 15%
13C enriched Phe in position 8, and the CMR spectra of these two products are compared. |
doi_str_mv | 10.1016/0006-291X(71)90025-8 |
format | Article |
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13C using the Fourier transform technique with proton noise decoupling. Chemical shift values have been studied as a function of pH. The peptide corresponding to the 1–15 sequence of ribonuclease has been synthesized both with normal and 15%
13C enriched Phe in position 8, and the CMR spectra of these two products are compared.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(71)90025-8</identifier><identifier>PMID: 5550801</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Carbon Isotopes ; Computers ; Histidine - analysis ; Hydrogen-Ion Concentration ; Magnetic Resonance Spectroscopy ; Peptides - analysis ; Phenylalanine - analysis ; Ribonucleases - analysis ; Stereoisomerism</subject><ispartof>Biochemical and biophysical research communications, 1971-03, Vol.42 (6), p.1148-1155</ispartof><rights>1971</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-e817948d6b52d335a20b016d2c49d28b2c2c4bfbecca5fb33766b49d2fb80dff3</citedby><cites>FETCH-LOGICAL-c357t-e817948d6b52d335a20b016d2c49d28b2c2c4bfbecca5fb33766b49d2fb80dff3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X71900258$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5550801$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Freedman, Murray H.</creatorcontrib><creatorcontrib>Cohen, Jack S.</creatorcontrib><creatorcontrib>Chaiken, Irwin M.</creatorcontrib><title>Carbon-13 Fourier transform nuclear magnetic resonance studies of peptides</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The carbon-13 nuclear magnetic resonance (CMR) spectra of several small peptides have been obtained at 25.1 MHz and natural abundance of
13C using the Fourier transform technique with proton noise decoupling. Chemical shift values have been studied as a function of pH. The peptide corresponding to the 1–15 sequence of ribonuclease has been synthesized both with normal and 15%
13C enriched Phe in position 8, and the CMR spectra of these two products are compared.</description><subject>Carbon Isotopes</subject><subject>Computers</subject><subject>Histidine - analysis</subject><subject>Hydrogen-Ion Concentration</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Peptides - analysis</subject><subject>Phenylalanine - analysis</subject><subject>Ribonucleases - analysis</subject><subject>Stereoisomerism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1971</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxDAUhYMo4zj6DxS6El1Ub9Kmj40gg-ODATcK7kIeNxJpmzFpBf-9rTO4dHUvnHPu5XyEnFK4okCLawAoUlbTt4uSXtYAjKfVHplTqCFlFPJ9Mv-zHJKjGD8AKM2LekZmnHOogM7J01IG5buUZsnKD8FhSPogu2h9aJNu0A3KkLTyvcPe6SRg9J3sNCaxH4zDmHibbHDTO4PxmBxY2UQ82c0FeV3dvSwf0vXz_ePydp3qjJd9ihUt67wyheLMZBmXDNRYxzCd14ZViulxU1ah1pJblWVlUahJsqoCY222IOfbu5vgPweMvWhd1Ng0skM_RFFBnTNastGYb406-BgDWrEJrpXhW1AQE0Ix8RETH1FS8YtQVGPsbHd_UC2av9CO2ajfbHUcS36NxETUDkcoxgXUvTDe_f_gB0BDgNg</recordid><startdate>19710319</startdate><enddate>19710319</enddate><creator>Freedman, Murray H.</creator><creator>Cohen, Jack S.</creator><creator>Chaiken, Irwin M.</creator><general>Elsevier Inc</general><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>19710319</creationdate><title>Carbon-13 Fourier transform nuclear magnetic resonance studies of peptides</title><author>Freedman, Murray H. ; Cohen, Jack S. ; Chaiken, Irwin M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-e817948d6b52d335a20b016d2c49d28b2c2c4bfbecca5fb33766b49d2fb80dff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1971</creationdate><topic>Carbon Isotopes</topic><topic>Computers</topic><topic>Histidine - analysis</topic><topic>Hydrogen-Ion Concentration</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Peptides - analysis</topic><topic>Phenylalanine - analysis</topic><topic>Ribonucleases - analysis</topic><topic>Stereoisomerism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Freedman, Murray H.</creatorcontrib><creatorcontrib>Cohen, Jack S.</creatorcontrib><creatorcontrib>Chaiken, Irwin M.</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Freedman, Murray H.</au><au>Cohen, Jack S.</au><au>Chaiken, Irwin M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Carbon-13 Fourier transform nuclear magnetic resonance studies of peptides</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1971-03-19</date><risdate>1971</risdate><volume>42</volume><issue>6</issue><spage>1148</spage><epage>1155</epage><pages>1148-1155</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The carbon-13 nuclear magnetic resonance (CMR) spectra of several small peptides have been obtained at 25.1 MHz and natural abundance of
13C using the Fourier transform technique with proton noise decoupling. Chemical shift values have been studied as a function of pH. The peptide corresponding to the 1–15 sequence of ribonuclease has been synthesized both with normal and 15%
13C enriched Phe in position 8, and the CMR spectra of these two products are compared.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>5550801</pmid><doi>10.1016/0006-291X(71)90025-8</doi><tpages>8</tpages></addata></record> |
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source | MEDLINE; Elsevier ScienceDirect Journals |
subjects | Carbon Isotopes Computers Histidine - analysis Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Peptides - analysis Phenylalanine - analysis Ribonucleases - analysis Stereoisomerism |
title | Carbon-13 Fourier transform nuclear magnetic resonance studies of peptides |
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