1ioj

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[[Image:1ioj.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ioj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ioj OCA], [http://www.ebi.ac.uk/pdbsum/1ioj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ioj RCSB]</span>
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'''HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES'''
'''HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES'''
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[[Category: Sparrow, J T.]]
[[Category: Sparrow, J T.]]
[[Category: Weisgraber, K H.]]
[[Category: Weisgraber, K H.]]
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[[Category: amphipathic helix]]
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[[Category: Amphipathic helix]]
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[[Category: apolipoprotein]]
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[[Category: Apolipoprotein]]
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[[Category: lcat activation]]
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[[Category: Lcat activation]]
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[[Category: lipid association]]
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[[Category: Lipid association]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:13:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:22:31 2008''
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Revision as of 17:13, 2 May 2008

Template:STRUCTURE 1ioj

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 Fri May 2 20:13:32 2008

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