Comparison of the stabilities and unfolding pathways of human apolipoprotein E isoforms by differential scanning calorimetry and circular dichroism

Differential scanning calorimetry and circular dichroism experiments were performed to study structural differences among the common isoforms of human apolipoprotein E (apoE2, apoE3, and apoE4) and their N-terminal, 22-kDa fragments. Here, we examine thermodynamic properties that characterize the st...

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Veröffentlicht in:	Biochimica et biophysica acta 2002-09, Vol.1584 (1), p.9-19
Hauptverfasser:	Acharya, Prathima, Segall, Mark L, Zaiou, Mohamed, Morrow, Julie, Weisgraber, Karl H, Phillips, Michael C, Lund-Katz, Sissel, Snow, Julian
Format:	Artikel
Sprache:	eng
Schlagworte:	Apolipoprotein E Apolipoprotein E2 Apolipoprotein E3 Apolipoprotein E4 Apolipoproteins E - chemistry Calorimetry, Differential Scanning Circular Dichroism Differential scanning calorimetry Humans Life Sciences Molecular Weight Protein Denaturation Protein Folding Protein Isoforms - chemistry Protein Structure, Secondary
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Zusammenfassung:	Differential scanning calorimetry and circular dichroism experiments were performed to study structural differences among the common isoforms of human apolipoprotein E (apoE2, apoE3, and apoE4) and their N-terminal, 22-kDa fragments. Here, we examine thermodynamic properties that characterize the structural differences among isoforms, and also differences in their unfolding behavior. The 22-kDa fragments and their full-length counterparts were found to exhibit similar differences in thermal stability (apoE4
ISSN:	1388-1981 0006-3002 1879-2618
DOI:	10.1016/S1388-1981(02)00263-9