Molecular Modeling Studies of Cholic Acid Host: Shape and Dimensions. 2

Abstract

Technical Report No. 3 on the three-dimensional 'clam' or cup shapes formed by two cholic acid molecules linked together by a substituted aromatic spacer had shown that the resulting cavities were of similar shape but different width, due to the flexible nature of this host system, with its sensitivity to minor bond rotations. In the L-arabinose binding protein, the binding pocket shape is cup-like, approximately 12-12.3 A long and 7.3 A wide. In order to mimic the sugar binding proteins, wherein the sugar hydroxyl groups are hydrogen bonded to the ionized amino acids of the protein through the heteroatoms, it was necessary to investigate the dimensions of the cholic acid host cavities more closely. (jg)

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Document Details

Document Type
Technical Report
Publication Date
May 21, 1990
Accession Number
ADA222074

Entities

People

  • Carol A. Venanzi
  • Suzanne M. Evans

Organizations

  • New Jersey Institute of Technology

Tags

Communities of Interest

  • C4I
  • Energy and Power Technologies

DTIC Thesaurus Topics

  • Abstracts
  • Amino Acids
  • Arabinose
  • Carrier Proteins
  • Chemistry
  • Classification
  • Dihedral Angle
  • Geometry
  • Hydrogen
  • Molecules
  • Monosaccharides
  • New Jersey
  • Proteins
  • Rotation
  • Security
  • Sugars
  • Three Dimensional

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  • Structural Dynamics.