1ioj
From Proteopedia
(New page: 200px<br /> <applet load="1ioj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ioj" /> '''HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURE...) |
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| - | [[Image:1ioj.gif|left|200px]]<br /> | + | [[Image:1ioj.gif|left|200px]]<br /><applet load="1ioj" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ioj" size=" | + | |
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'''HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES'''<br /> | '''HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein | + | Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distributed mainly in high and very low density lipoprotein. In this report we present the nuclear magnetic resonance spectra of native apoC-I and synthetic apoC-I, containing selected 15N-labelled amino acids, in the presence of sodium dodecyl sulfate. The proton resonances of apoC-I are assigned and the secondary structure is estimated from the difference of measured alpha-proton chemical shifts to random coil values and the observed NOE interactions. According to these data apoC-I forms two helices, Val-4-Lys-30 and Leu-34-Lys-52, linked by an unstructured region Gln-31-Glu-33. The N-terminal segments of each helix, Val-4-Gly-15 and Leu-34-Met-38, appear to be more flexible than the helical core regions Asn-16-Lys-30 and Arg-39-Lys-52. |
==About this Structure== | ==About this Structure== | ||
| - | 1IOJ 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:// | + | 1IOJ 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=1IOJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cushley, R | + | [[Category: Cushley, R J.]] |
[[Category: Rozek, A.]] | [[Category: Rozek, A.]] | ||
| - | [[Category: Sparrow, J | + | [[Category: Sparrow, J T.]] |
| - | [[Category: Weisgraber, K | + | [[Category: Weisgraber, K H.]] |
[[Category: amphipathic helix]] | [[Category: amphipathic helix]] | ||
[[Category: apolipoprotein]] | [[Category: apolipoprotein]] | ||
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[[Category: lipid association]] | [[Category: lipid association]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:56 2008'' |
Revision as of 11:13, 21 February 2008
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HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES
Overview
Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distributed mainly in high and very low density lipoprotein. In this report we present the nuclear magnetic resonance spectra of native apoC-I and synthetic apoC-I, containing selected 15N-labelled amino acids, in the presence of sodium dodecyl sulfate. The proton resonances of apoC-I are assigned and the secondary structure is estimated from the difference of measured alpha-proton chemical shifts to random coil values and the observed NOE interactions. According to these data apoC-I forms two helices, Val-4-Lys-30 and Leu-34-Lys-52, linked by an unstructured region Gln-31-Glu-33. The N-terminal segments of each helix, Val-4-Gly-15 and Leu-34-Met-38, appear to be more flexible than the helical core regions Asn-16-Lys-30 and Arg-39-Lys-52.
About this Structure
1IOJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate., Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ, Biochem Cell Biol. 1998;76(2-3):267-75. PMID:9923695
Page seeded by OCA on Thu Feb 21 13:13:56 2008
