Accession Number:

ADA220952

Title:

Molecular Modeling Studies of Cholic Acid Host: Shape and Dimensions

Descriptive Note:

Technical rept.

Corporate Author:

NEW JERSEY INST OF TECH NEWARK DIV OF CHEMISTRY

Personal Author(s):

Report Date:

1990-04-18

Pagination or Media Count:

14.0

Abstract:

The literature of sugar binding proteins, in particular the protein binding L-arabinose, indicates that the binding pocket shape is cup-like, with the hydroxyl groups of the L-arabinose hydrogen bonding to the ionized amino acids of the protein through the heteroatoms, with or without an intervening water network fig.1 Measurements of the L-arabinose binding protein cavity, taken from the computer graphics representation of the X-ray crytallographic coordinates, indicate that the cavity is approximately 12-12.3 A long and 7.3 A wide Fig 2. To evaluate the dimensions of a cavity created by two cholic acid molecules linked together by a substituted aromatic spacer, several starting structures for this cup or clam shape of the host system were generated. The study of this host system considers both the torsional angles of the cholic acids side chain and the torsional angles linking the carboxamide group of the cholic acid molecule to the benzyl group. Keywords Chemical bonding Binding sites Molecular interaction.

Subject Categories:

  • Organic Chemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE