Title : Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution.

Pub. Date : 2002 Apr 24

PMID : 12062424






5 Functional Relationships(s)
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1 The apolipoprotein A-I (apoA-I) solution structure in the presence of sodium dodecyl sulfate (SDS) was determined by combination of chemical shift index and torsion angle likelihood obtained from shift and sequence similarity methods. Sodium Dodecyl Sulfate apolipoprotein A1 Homo sapiens
2 The apolipoprotein A-I (apoA-I) solution structure in the presence of sodium dodecyl sulfate (SDS) was determined by combination of chemical shift index and torsion angle likelihood obtained from shift and sequence similarity methods. Sodium Dodecyl Sulfate apolipoprotein A1 Homo sapiens
3 The apolipoprotein A-I (apoA-I) solution structure in the presence of sodium dodecyl sulfate (SDS) was determined by combination of chemical shift index and torsion angle likelihood obtained from shift and sequence similarity methods. Sodium Dodecyl Sulfate apolipoprotein A1 Homo sapiens
4 The apolipoprotein A-I (apoA-I) solution structure in the presence of sodium dodecyl sulfate (SDS) was determined by combination of chemical shift index and torsion angle likelihood obtained from shift and sequence similarity methods. Sodium Dodecyl Sulfate apolipoprotein A1 Homo sapiens
5 ApoA-I is a monomer in the SDS complex and no evidence of interhelical interactions is found. Sodium Dodecyl Sulfate apolipoprotein A1 Homo sapiens