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[[Image:1ale.jpg|left|200px]]<br /><applet load="1ale" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ale" />
'''CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY'''<br />


==Overview==
==CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY==
Peptides corresponding to the proposed lipid-binding domains of human, apolipoprotein C-I, residues 7-24 (ALDKLKEFGNTLEDKARE) and 35-53, (SAKMREWFSETFQKVKEKL), were studied by CD and two-dimensional 1H NMR, spectroscopy. Sodium dodecyl sulfate (SDS) was used to model the, lipoprotein environment. Analysis of the CD data shows that both peptides, lack well-defined structure in aqueous solution but adopt helical, ordered, structures upon the addition of SDS. The helical nature of the peptides in, the presence of SDS was confirmed by H alpha secondary shifts. A total of, 199 (apoC-I(7-24)) and 266 (apoC-I(35-53)) distance restraints were used, in distance geometry and simulated annealing calculations to generate, average structures for both peptides in aqueous solutions containing SDS., The backbone (N, C alpha, C = O) RMSD from the average structure of an, ensemble of 20 structures was 0.73 +/- 0.22 and 0.48 +/- 0.14 A for, apoC-I(7-24) and apoC-I(35-53), respectively. In the presence of SDS, the, distance geometry and simulated annealing calculations show that both, peptides adopt well-defined amphipathic helices with distinct hydrophobic, and hydrophilic faces. The calculated structures are discussed relative to, predicted structures. Comparing our CD and NMR results for the apoC-I, fragments in SDS with CD results of others obtained in the presence of, dimyristoylphosphatidylcholine indicates that SDS may be a better model of, the lipoprotein environment.
<StructureSection load='1ale' size='340' side='right'caption='[[1ale]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ale]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ale FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ale OCA], [https://pdbe.org/1ale PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ale RCSB], [https://www.ebi.ac.uk/pdbsum/1ale PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ale ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/APOC1_HUMAN APOC1_HUMAN] Appears to modulate the interaction of APOE with beta-migrating VLDL and inhibit binding of beta-VLDL to the LDL receptor-related protein. Binds free fatty acids and reduces their intracellular esterification.<ref>PMID:17339654</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptides corresponding to the proposed lipid-binding domains of human apolipoprotein C-I, residues 7-24 (ALDKLKEFGNTLEDKARE) and 35-53 (SAKMREWFSETFQKVKEKL), were studied by CD and two-dimensional 1H NMR spectroscopy. Sodium dodecyl sulfate (SDS) was used to model the lipoprotein environment. Analysis of the CD data shows that both peptides lack well-defined structure in aqueous solution but adopt helical, ordered structures upon the addition of SDS. The helical nature of the peptides in the presence of SDS was confirmed by H alpha secondary shifts. A total of 199 (apoC-I(7-24)) and 266 (apoC-I(35-53)) distance restraints were used in distance geometry and simulated annealing calculations to generate average structures for both peptides in aqueous solutions containing SDS. The backbone (N, C alpha, C = O) RMSD from the average structure of an ensemble of 20 structures was 0.73 +/- 0.22 and 0.48 +/- 0.14 A for apoC-I(7-24) and apoC-I(35-53), respectively. In the presence of SDS, the distance geometry and simulated annealing calculations show that both peptides adopt well-defined amphipathic helices with distinct hydrophobic and hydrophilic faces. The calculated structures are discussed relative to predicted structures. Comparing our CD and NMR results for the apoC-I fragments in SDS with CD results of others obtained in the presence of dimyristoylphosphatidylcholine indicates that SDS may be a better model of the lipoprotein environment.


==About this Structure==
Conformation of two peptides corresponding to human apolipoprotein C-I residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and NMR spectroscopy.,Rozek A, Buchko GW, Cushley RJ Biochemistry. 1995 Jun 6;34(22):7401-8. PMID:7779782<ref>PMID:7779782</ref>
1ALE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALE OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Conformation of two peptides corresponding to human apolipoprotein C-I residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and NMR spectroscopy., Rozek A, Buchko GW, Cushley RJ, Biochemistry. 1995 Jun 6;34(22):7401-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7779782 7779782]
</div>
<div class="pdbe-citations 1ale" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Buchko, G.W.]]
[[Category: Buchko GW]]
[[Category: Cushley, R.J.]]
[[Category: Cushley RJ]]
[[Category: Rozek, A.]]
[[Category: Rozek A]]
[[Category: apolipoprotein]]
 
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