Chemical synthesis and structure elucidation of bovine κ-casein (1–44)
The caseins (α s1, α s2, β, and κ) are phosphoproteins present in bovine milk that have been studied for over a century and whose structures remain obscure. Here we describe the chemical synthesis and structure elucidation of the N-terminal segment (1–44) of bovine κ-casein, the protein which mainta...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2006-02, Vol.340 (4), p.1098-1103 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Bansal, Paramjit S. Grieve, Paul A. Marschke, Ronald J. Daly, Norelle L. McGhie, Emily Craik, David J. Alewood, Paul F. |
| description | The caseins (α
s1, α
s2, β, and κ) are phosphoproteins present in bovine milk that have been studied for over a century and whose structures remain obscure. Here we describe the chemical synthesis and structure elucidation of the N-terminal segment (1–44) of bovine κ-casein, the protein which maintains the micellar structure of the caseins. κ-Casein (1–44) was synthesised by highly optimised Boc solid-phase peptide chemistry and characterised by mass spectrometry. Structure elucidation was carried out by circular dichroism and nuclear magnetic resonance spectroscopy. CD analysis demonstrated that the segment was ill defined in aqueous medium but in 30% trifluoroethanol it exhibited considerable helical structure. Further, NMR analysis showed the presence of a helical segment containing 26 residues which extends from Pro
8 to Arg
34. This is the first report which demonstrates extensive secondary structure within the casein class of proteins. |
| doi_str_mv | 10.1016/j.bbrc.2005.12.115 |
| format | Article |
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s1, α
s2, β, and κ) are phosphoproteins present in bovine milk that have been studied for over a century and whose structures remain obscure. Here we describe the chemical synthesis and structure elucidation of the N-terminal segment (1–44) of bovine κ-casein, the protein which maintains the micellar structure of the caseins. κ-Casein (1–44) was synthesised by highly optimised Boc solid-phase peptide chemistry and characterised by mass spectrometry. Structure elucidation was carried out by circular dichroism and nuclear magnetic resonance spectroscopy. CD analysis demonstrated that the segment was ill defined in aqueous medium but in 30% trifluoroethanol it exhibited considerable helical structure. Further, NMR analysis showed the presence of a helical segment containing 26 residues which extends from Pro
8 to Arg
34. This is the first report which demonstrates extensive secondary structure within the casein class of proteins.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2005.12.115</identifier><identifier>PMID: 16403439</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>2D NMR ; Amino Acid Sequence ; Animals ; Caseins - chemical synthesis ; Caseins - chemistry ; Caseins - ultrastructure ; Cattle ; Computer Simulation ; Crystallography ; Helical structure ; Milk protein ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Solid-phase peptide synthesis ; κ-Casein</subject><ispartof>Biochemical and biophysical research communications, 2006-02, Vol.340 (4), p.1098-1103</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c354t-8c2e2cd9279cc9a6fed3a88dfa72833f5b460d8c6ee2bf2066883db80a90668a3</citedby><cites>FETCH-LOGICAL-c354t-8c2e2cd9279cc9a6fed3a88dfa72833f5b460d8c6ee2bf2066883db80a90668a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2005.12.115$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27911,27912,45982</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16403439$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bansal, Paramjit S.</creatorcontrib><creatorcontrib>Grieve, Paul A.</creatorcontrib><creatorcontrib>Marschke, Ronald J.</creatorcontrib><creatorcontrib>Daly, Norelle L.</creatorcontrib><creatorcontrib>McGhie, Emily</creatorcontrib><creatorcontrib>Craik, David J.</creatorcontrib><creatorcontrib>Alewood, Paul F.</creatorcontrib><title>Chemical synthesis and structure elucidation of bovine κ-casein (1–44)</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The caseins (α
s1, α
s2, β, and κ) are phosphoproteins present in bovine milk that have been studied for over a century and whose structures remain obscure. Here we describe the chemical synthesis and structure elucidation of the N-terminal segment (1–44) of bovine κ-casein, the protein which maintains the micellar structure of the caseins. κ-Casein (1–44) was synthesised by highly optimised Boc solid-phase peptide chemistry and characterised by mass spectrometry. Structure elucidation was carried out by circular dichroism and nuclear magnetic resonance spectroscopy. CD analysis demonstrated that the segment was ill defined in aqueous medium but in 30% trifluoroethanol it exhibited considerable helical structure. Further, NMR analysis showed the presence of a helical segment containing 26 residues which extends from Pro
8 to Arg
34. This is the first report which demonstrates extensive secondary structure within the casein class of proteins.</description><subject>2D NMR</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Caseins - chemical synthesis</subject><subject>Caseins - chemistry</subject><subject>Caseins - ultrastructure</subject><subject>Cattle</subject><subject>Computer Simulation</subject><subject>Crystallography</subject><subject>Helical structure</subject><subject>Milk protein</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Solid-phase peptide synthesis</subject><subject>κ-Casein</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1Kw0AUhQdRbK2-gAvJSnSReGcmnU7AjRR_CgU3Cu6GycwNnZImdSYpdOc7-DY-hA_hk5jQgjtX9yy-c-B-hJxTSChQcbNM8tybhAGME8oSSscHZEghg5hRSA_JEABEzDL6NiAnISwBKE1FdkwGVKTAU54NyWy6wJUzuozCtmoWGFyIdGWj0PjWNK3HCMvWOKsbV1dRXUR5vXEVRt9fsdEBXRVd0Z-PzzS9PiVHhS4Dnu3viLw-3L9Mn-L58-NsejePDR-nTSwNQ2ZsxiaZMZkWBVqupbSFnjDJeTHOUwFWGoHI8oKBEFJym0vQWZ81H5HL3e7a1-8thkatXDBYlrrCug1qAmIiuGQdyHag8XUIHgu19m6l_VZRUL1AtVS9QNULVJSpTmBXutivt_kK7V9lb6wDbncAdj9uHHoVjMPKoHUeTaNs7f7b_wW2JoKh</recordid><startdate>20060224</startdate><enddate>20060224</enddate><creator>Bansal, Paramjit S.</creator><creator>Grieve, Paul A.</creator><creator>Marschke, Ronald J.</creator><creator>Daly, Norelle L.</creator><creator>McGhie, Emily</creator><creator>Craik, David J.</creator><creator>Alewood, Paul F.</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>20060224</creationdate><title>Chemical synthesis and structure elucidation of bovine κ-casein (1–44)</title><author>Bansal, Paramjit S. ; Grieve, Paul A. ; Marschke, Ronald J. ; Daly, Norelle L. ; McGhie, Emily ; Craik, David J. ; Alewood, Paul F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c354t-8c2e2cd9279cc9a6fed3a88dfa72833f5b460d8c6ee2bf2066883db80a90668a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>2D NMR</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Caseins - chemical synthesis</topic><topic>Caseins - chemistry</topic><topic>Caseins - ultrastructure</topic><topic>Cattle</topic><topic>Computer Simulation</topic><topic>Crystallography</topic><topic>Helical structure</topic><topic>Milk protein</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Solid-phase peptide synthesis</topic><topic>κ-Casein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bansal, Paramjit S.</creatorcontrib><creatorcontrib>Grieve, Paul A.</creatorcontrib><creatorcontrib>Marschke, Ronald J.</creatorcontrib><creatorcontrib>Daly, Norelle L.</creatorcontrib><creatorcontrib>McGhie, Emily</creatorcontrib><creatorcontrib>Craik, David J.</creatorcontrib><creatorcontrib>Alewood, Paul F.</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>Bansal, Paramjit S.</au><au>Grieve, Paul A.</au><au>Marschke, Ronald J.</au><au>Daly, Norelle L.</au><au>McGhie, Emily</au><au>Craik, David J.</au><au>Alewood, Paul F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chemical synthesis and structure elucidation of bovine κ-casein (1–44)</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-02-24</date><risdate>2006</risdate><volume>340</volume><issue>4</issue><spage>1098</spage><epage>1103</epage><pages>1098-1103</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The caseins (α
s1, α
s2, β, and κ) are phosphoproteins present in bovine milk that have been studied for over a century and whose structures remain obscure. Here we describe the chemical synthesis and structure elucidation of the N-terminal segment (1–44) of bovine κ-casein, the protein which maintains the micellar structure of the caseins. κ-Casein (1–44) was synthesised by highly optimised Boc solid-phase peptide chemistry and characterised by mass spectrometry. Structure elucidation was carried out by circular dichroism and nuclear magnetic resonance spectroscopy. CD analysis demonstrated that the segment was ill defined in aqueous medium but in 30% trifluoroethanol it exhibited considerable helical structure. Further, NMR analysis showed the presence of a helical segment containing 26 residues which extends from Pro
8 to Arg
34. This is the first report which demonstrates extensive secondary structure within the casein class of proteins.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16403439</pmid><doi>10.1016/j.bbrc.2005.12.115</doi><tpages>6</tpages></addata></record> |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | 2D NMR Amino Acid Sequence Animals Caseins - chemical synthesis Caseins - chemistry Caseins - ultrastructure Cattle Computer Simulation Crystallography Helical structure Milk protein Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Secondary Solid-phase peptide synthesis κ-Casein |
| title | Chemical synthesis and structure elucidation of bovine κ-casein (1–44) |
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