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Titolo:
CONFORMATIONAL-ANALYSIS OF ARACHIDONIC AND RELATED FATTY-ACIDS USING MOLECULAR-DYNAMICS SIMULATIONS
Autore:
RICH MR;
Indirizzi:
NYU,DEPT BIOL,WASHINGTON SQ NEW YORK NY 10003
Titolo Testata:
Biochimica et biophysica acta
fascicolo: 1, volume: 1178, anno: 1993,
pagine: 87 - 96
SICI:
0006-3002(1993)1178:1<87:COAARF>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN KINASE-C; 2ND MESSENGER; POTASSIUM CHANNELS; ACTIVATION; CELLS; PHOSPHOLIPIDS; BILAYERS; CHAINS;
Keywords:
ARACHIDONIC ACID; FATTY ACID; CONFORMATIONAL ANALYSIS; COMPUTER SIMULATION; MOLECULAR DYNAMICS SIMULATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
M.R. Rich, "CONFORMATIONAL-ANALYSIS OF ARACHIDONIC AND RELATED FATTY-ACIDS USING MOLECULAR-DYNAMICS SIMULATIONS", Biochimica et biophysica acta, 1178(1), 1993, pp. 87-96

Abstract

Arachidonic acid has recently gained attention as a result of currentevidence indicating that it may play the role of a 'second messenger'in signal transduction processes. In order to gain insight into the mechanism behind its action, quenched molecular dynamics simulations were performed on arachidonic (20:4) and related fatty acids: linoleic (18:2), oleic (18:1), arachidic (20:0), and stearic (18:0). The angle-iron structure, representative of arachidonic acid in the crystal or very-low-temperature state, readily gave way at higher temperature to a dominant hairpin structure whereby the COOH end of arachidonic acid comes into close proximity with the C14-15 pi-bond resulting in a packedpi-bond-rich loop. The lowest energy conformer for arachidonic acid was found to bc 10.65 kcal/mol below that of the energy-minimized crystal structure. In the case of saturated fatty acids, the crystal all-trans conformation remained the lowest energy form. Analysis of conformational energy contours for carbon-carbon torsion angles representativeof fatty acids suggest that the flexibility of arachidonic acid is, in part, a result of the relative torsional freedom of C-C (single) bonds located between or adjacent to C=C (double) bonds. It is hypothesized that the ability of arachidonic acid to form packed structures withcurved regions containing pi-bonds may allow for hydrophobic interactions with proteins, and/or hydrogen bonding between the pi-bonds of arachidonic acid and polar groups of the protein structures.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 05:12:32