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Volume 270, Number 16, Issue of April 21, pp. 9192-9196, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Sonia Bauelos , José Luis R. Arrondo , Félix M. Goi , Greta Pifat

The secondary structure of human apolipoprotein B at 37 °C is estimated to be 24% -helix, 23% -sheet, 6% -turns, 24% unordered structure, and 24% ``-strands,'' characterized by a band around 1618 cm, and consistent with extended string-like chains in contact with the lipid moiety not forming -sheets. When cooled to a temperature below the cholesteryl ester transition at 30 °C, the ordering of the low density lipoprotein core results in reversible changes in the protein conformation, decreasing the apparent amount of -helix, -strand, and unordered structure below 30 °C and increasing -sheet and -turns. Lowering the ionic strength affects the core-associated transitions, shifting their temperature from 30 to 20 °C, and modifying protein conformation below the transition. An additional thermal event is observed at 75 °C, leading to irreversible protein denaturation. In the broad temperature range between the 30 and 75 °C transitions, apolipoprotein B is stable toward both temperature and ionic strength changes. After thermal denaturation, the protein retains a certain degree of ordered structure.

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