A. Rozek et al., Sequence-specific H-1 NMR resonance assignments and secondary structure ofhuman apolipoprotein C-I in the presence of sodium dodecyl sulfate, BIOC CELL B, 76(2-3), 1998, pp. 267-275
Citations number
41
Categorie Soggetti
Cell & Developmental Biology
Journal title
BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE
Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distri
buted mainly in high and very low density lipoprotein. In this report we pr
esent the nuclear magnetic resonance spectra of native apoC-I and synthetic
apoC-I, containing selected N-15-labelled amino acids, in the presence of
sodium dodecyl sulfate. The proton resonances of apoC-I are assigned and th
e secondary structure is estimated from the difference of measured cc-proto
n 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-L
ys-52, linked by an unstructured region Gln-31-Glu-33. The N-terminal segme
nts of each helix, Val-4-Gly-15 and Leu-34-Met-38, appear to be more flexib
le than the helical core regions Asn-16-Lys-30 and Arg-39-Lys-52.