1ioj
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(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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Revision as of 15:26, 12 November 2007
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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
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