Conformation Of The Lecithin Molecule With Attached Water Molecules

Abstract

CNDO/2 studies on the conformation of the α chain of lecithin indicated a strong preference for a gauche-gauche arrangement about the phosphodiester group. Folding the α chain about[Figure not available: see fulltext.] and α4 was energetically very favorable. Hydration of the same segment revealed three levels of water-binding energies. The ion-dipole interactions of water and the choline moiety were energetically non-substantial. In contrast, binding of water to the unesterified phosphate oxygens produced the highest enthalpies. Attachment of water to the esterified phosphate oxygens or the ester oxygens of the β chain resulted in intermediate binding strengths. By investigating complete incorporation of nine water molecules into a chosen lipid structure, a plausible lecithin-water geometry was deduced for a liquid crystalline system. © 1981 Forum Press, Inc.

Department(s)

Chemistry

Second Department

Physics

International Standard Serial Number (ISSN)

1573-0689; 0092-0606

Document Type

Article - Journal

Document Version

Citation

File Type

text

Language(s)

English

Rights

© 2023 Springer, All rights reserved.

Publication Date

01 Dec 1981

Link to Full Text

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