Dynamics of Palmitic Acid Complexed with Rat Intestinal Fatty Acid Binding Protein
Dynamics of palmitic acid (PA), isotopically enriched with 13C at the second, seventh, or terminal methyl position, were investigated by 13C NMR. Relaxation measurements were made on PA bound to recombinant rat intestinal fatty acid binding protein (I-FABP) at pH 5.5 and 23 °C, and, for comparison,...
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| Veröffentlicht in: | Biochemistry (Easton) 1999-02, Vol.38 (5), p.1554-1561 |
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| creator | Zhu, Lingyang Kurian, Elizabeth Prendergast, Franklyn G Kemple, Marvin D |
| description | Dynamics of palmitic acid (PA), isotopically enriched with 13C at the second, seventh, or terminal methyl position, were investigated by 13C NMR. Relaxation measurements were made on PA bound to recombinant rat intestinal fatty acid binding protein (I-FABP) at pH 5.5 and 23 °C, and, for comparison, on PA incorporated into 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine (MPPC) micelles, and dissolved in methanol. The 13C relaxation data, T 1, and steady-state nuclear Overhauser effect (NOE) obtained at two different magnetic fields were interpreted using the model-free approach [Lipari, G., and Szabo, A. (1982) J. Am. Chem. Soc. 104, 4546−4559]. The overall rotational correlation time of the fatty acid·protein complex was 2.5 ± 0.4 ns, which is substantially less than the value expected for the protein itself (>6 ns). Order parameters (S 2), which are a measure of the amplitude of the internal motion of individual C−H vectors with respect to the PA molecule, while largest for C-2 and smallest for the methyl carbon, were relatively small ( |
| doi_str_mv | 10.1021/bi982087v |
| format | Article |
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Relaxation measurements were made on PA bound to recombinant rat intestinal fatty acid binding protein (I-FABP) at pH 5.5 and 23 °C, and, for comparison, on PA incorporated into 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine (MPPC) micelles, and dissolved in methanol. The 13C relaxation data, T 1, and steady-state nuclear Overhauser effect (NOE) obtained at two different magnetic fields were interpreted using the model-free approach [Lipari, G., and Szabo, A. (1982) J. Am. Chem. Soc. 104, 4546−4559]. The overall rotational correlation time of the fatty acid·protein complex was 2.5 ± 0.4 ns, which is substantially less than the value expected for the protein itself (>6 ns). Order parameters (S 2), which are a measure of the amplitude of the internal motion of individual C−H vectors with respect to the PA molecule, while largest for C-2 and smallest for the methyl carbon, were relatively small (<0.4) in the protein complex. S 2 values for given C−H vectors also were smaller for PA in the MPPC micelles and in methanol than in the protein complex. Correlation times reflective of the time scale of the internal motion of the C−H vectors were in all cases <60 ps. These results support the view that the fatty acid is not rigidly anchored within the I-FABP binding pocket, but rather has considerable freedom to move within the pocket.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi982087v</identifier><identifier>PMID: 9931022</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Carbon Isotopes ; Carrier Proteins - chemistry ; Computer Simulation ; Fatty Acid-Binding Protein 7 ; Fatty Acid-Binding Proteins ; Fatty Acids - chemistry ; Intestines - chemistry ; Macromolecular Substances ; Mathematical Computing ; Methanol - chemistry ; Micelles ; Models, Molecular ; Myelin P2 Protein - chemistry ; Neoplasm Proteins ; Nerve Tissue Proteins ; Nuclear Magnetic Resonance, Biomolecular ; Palmitic Acid - chemistry ; Phosphatidylcholines - chemistry ; Rats ; Thermodynamics</subject><ispartof>Biochemistry (Easton), 1999-02, Vol.38 (5), p.1554-1561</ispartof><rights>Copyright © 1999 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a348t-505d037460ce16cf0002cfbe8523310729891d69aa03660247cd9e2e8eeb5fbf3</citedby><cites>FETCH-LOGICAL-a348t-505d037460ce16cf0002cfbe8523310729891d69aa03660247cd9e2e8eeb5fbf3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi982087v$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi982087v$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9931022$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhu, Lingyang</creatorcontrib><creatorcontrib>Kurian, Elizabeth</creatorcontrib><creatorcontrib>Prendergast, Franklyn G</creatorcontrib><creatorcontrib>Kemple, Marvin D</creatorcontrib><title>Dynamics of Palmitic Acid Complexed with Rat Intestinal Fatty Acid Binding Protein</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Dynamics of palmitic acid (PA), isotopically enriched with 13C at the second, seventh, or terminal methyl position, were investigated by 13C NMR. Relaxation measurements were made on PA bound to recombinant rat intestinal fatty acid binding protein (I-FABP) at pH 5.5 and 23 °C, and, for comparison, on PA incorporated into 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine (MPPC) micelles, and dissolved in methanol. The 13C relaxation data, T 1, and steady-state nuclear Overhauser effect (NOE) obtained at two different magnetic fields were interpreted using the model-free approach [Lipari, G., and Szabo, A. (1982) J. Am. Chem. Soc. 104, 4546−4559]. The overall rotational correlation time of the fatty acid·protein complex was 2.5 ± 0.4 ns, which is substantially less than the value expected for the protein itself (>6 ns). Order parameters (S 2), which are a measure of the amplitude of the internal motion of individual C−H vectors with respect to the PA molecule, while largest for C-2 and smallest for the methyl carbon, were relatively small (<0.4) in the protein complex. S 2 values for given C−H vectors also were smaller for PA in the MPPC micelles and in methanol than in the protein complex. Correlation times reflective of the time scale of the internal motion of the C−H vectors were in all cases <60 ps. These results support the view that the fatty acid is not rigidly anchored within the I-FABP binding pocket, but rather has considerable freedom to move within the pocket.</description><subject>Animals</subject><subject>Carbon Isotopes</subject><subject>Carrier Proteins - chemistry</subject><subject>Computer Simulation</subject><subject>Fatty Acid-Binding Protein 7</subject><subject>Fatty Acid-Binding Proteins</subject><subject>Fatty Acids - chemistry</subject><subject>Intestines - chemistry</subject><subject>Macromolecular Substances</subject><subject>Mathematical Computing</subject><subject>Methanol - chemistry</subject><subject>Micelles</subject><subject>Models, Molecular</subject><subject>Myelin P2 Protein - chemistry</subject><subject>Neoplasm Proteins</subject><subject>Nerve Tissue Proteins</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Palmitic Acid - chemistry</subject><subject>Phosphatidylcholines - chemistry</subject><subject>Rats</subject><subject>Thermodynamics</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM1OwzAQhC0EKqVw4AGQfAGJQ8BxYjs-QqFQUUFVCgculuM44JKfEjvQvj1GqXritFrNt7OjAeA4RBchwuFlaniCUcK-d0A_JBgFMedkF_QRQjTAnKJ9cGDtwq8xYnEP9DiP_CHug9nNupKlURbWOZzKojTOKHilTAaHdbks9Epn8Me4DziTDo4rp60zlSzgSDq37sBrU2WmeofTpnbaVIdgL5eF1UebOQAvo9v58D6YPN2Nh1eTQEZx4gKCSIYiFlOkdEhV7sNhlac6ITjy4RjmCQ8zyqVEEaUIx0xlXGOdaJ2SPM2jATjrfJdN_dX6XKI0VumikJWuWysoJ4zSGHvwvANVU1vb6FwsG1PKZi1CJP76E9v-PHuyMW3TUmdbclOY14NON9bp1VaWzaegLGJEzKfP4jWOHh_eUCimnj_teKmsWNRt47uz__z9BW3ShLk</recordid><startdate>19990202</startdate><enddate>19990202</enddate><creator>Zhu, Lingyang</creator><creator>Kurian, Elizabeth</creator><creator>Prendergast, Franklyn G</creator><creator>Kemple, Marvin D</creator><general>American Chemical Society</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>19990202</creationdate><title>Dynamics of Palmitic Acid Complexed with Rat Intestinal Fatty Acid Binding Protein</title><author>Zhu, Lingyang ; Kurian, Elizabeth ; Prendergast, Franklyn G ; Kemple, Marvin D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a348t-505d037460ce16cf0002cfbe8523310729891d69aa03660247cd9e2e8eeb5fbf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Carbon Isotopes</topic><topic>Carrier Proteins - chemistry</topic><topic>Computer Simulation</topic><topic>Fatty Acid-Binding Protein 7</topic><topic>Fatty Acid-Binding Proteins</topic><topic>Fatty Acids - chemistry</topic><topic>Intestines - chemistry</topic><topic>Macromolecular Substances</topic><topic>Mathematical Computing</topic><topic>Methanol - chemistry</topic><topic>Micelles</topic><topic>Models, Molecular</topic><topic>Myelin P2 Protein - chemistry</topic><topic>Neoplasm Proteins</topic><topic>Nerve Tissue Proteins</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Palmitic Acid - chemistry</topic><topic>Phosphatidylcholines - chemistry</topic><topic>Rats</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhu, Lingyang</creatorcontrib><creatorcontrib>Kurian, Elizabeth</creatorcontrib><creatorcontrib>Prendergast, Franklyn G</creatorcontrib><creatorcontrib>Kemple, Marvin D</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>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhu, Lingyang</au><au>Kurian, Elizabeth</au><au>Prendergast, Franklyn G</au><au>Kemple, Marvin D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dynamics of Palmitic Acid Complexed with Rat Intestinal Fatty Acid Binding Protein</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1999-02-02</date><risdate>1999</risdate><volume>38</volume><issue>5</issue><spage>1554</spage><epage>1561</epage><pages>1554-1561</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Dynamics of palmitic acid (PA), isotopically enriched with 13C at the second, seventh, or terminal methyl position, were investigated by 13C NMR. Relaxation measurements were made on PA bound to recombinant rat intestinal fatty acid binding protein (I-FABP) at pH 5.5 and 23 °C, and, for comparison, on PA incorporated into 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine (MPPC) micelles, and dissolved in methanol. The 13C relaxation data, T 1, and steady-state nuclear Overhauser effect (NOE) obtained at two different magnetic fields were interpreted using the model-free approach [Lipari, G., and Szabo, A. (1982) J. Am. Chem. Soc. 104, 4546−4559]. The overall rotational correlation time of the fatty acid·protein complex was 2.5 ± 0.4 ns, which is substantially less than the value expected for the protein itself (>6 ns). Order parameters (S 2), which are a measure of the amplitude of the internal motion of individual C−H vectors with respect to the PA molecule, while largest for C-2 and smallest for the methyl carbon, were relatively small (<0.4) in the protein complex. S 2 values for given C−H vectors also were smaller for PA in the MPPC micelles and in methanol than in the protein complex. Correlation times reflective of the time scale of the internal motion of the C−H vectors were in all cases <60 ps. These results support the view that the fatty acid is not rigidly anchored within the I-FABP binding pocket, but rather has considerable freedom to move within the pocket.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>9931022</pmid><doi>10.1021/bi982087v</doi><tpages>8</tpages></addata></record> |
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| subjects | Animals Carbon Isotopes Carrier Proteins - chemistry Computer Simulation Fatty Acid-Binding Protein 7 Fatty Acid-Binding Proteins Fatty Acids - chemistry Intestines - chemistry Macromolecular Substances Mathematical Computing Methanol - chemistry Micelles Models, Molecular Myelin P2 Protein - chemistry Neoplasm Proteins Nerve Tissue Proteins Nuclear Magnetic Resonance, Biomolecular Palmitic Acid - chemistry Phosphatidylcholines - chemistry Rats Thermodynamics |
| title | Dynamics of Palmitic Acid Complexed with Rat Intestinal Fatty Acid Binding Protein |
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