Title : Conformation of human serum apolipoprotein A-I(166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence for specific peptide-SDS interactions.

Pub. Date : 1996 Jun 11

PMID : 8664326






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Conformation of human serum apolipoprotein A-I(166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Sodium Dodecyl Sulfate apolipoprotein A1 Homo sapiens
2 The segment, YSDELRQRLAARLEALKENG, corresponding to residues 166 to 185 of human serum apolipoprotein A-I, was studied by circular dichroism and NMR spectroscopy in sodium dodecyl sulfate and dodecylphosphocholine micelles. Sodium Dodecyl Sulfate apolipoprotein A1 Homo sapiens
3 2-Dimensional NOESY, TOCSY and DQF-COSY spectra of apoA-I(166-185) in perdeuterated sodium dodecyl sulfate (SDS-d25) and dodecylphosphocholine (DPC-d38) micelles were collected at a peptide/SDS (DPC) ratio of 1:40. Sodium Dodecyl Sulfate apolipoprotein A1 Homo sapiens
4 2-Dimensional NOESY, TOCSY and DQF-COSY spectra of apoA-I(166-185) in perdeuterated sodium dodecyl sulfate (SDS-d25) and dodecylphosphocholine (DPC-d38) micelles were collected at a peptide/SDS (DPC) ratio of 1:40. Sodium Dodecyl Sulfate apolipoprotein A1 Homo sapiens
5 Similar CD spectra and NOE connectivity patterns were observed for apoA-I(166-185) in SDS and DPC, indicating a similar helical conformation in both. Sodium Dodecyl Sulfate apolipoprotein A1 Homo sapiens