Amino Acid Sequence Transfer Operators and Metric Space Distortions of Proteins,

Abstract

Physical and chemical studies of protein dynamics often yield nonlinear distortions and multiplicities of time scales which are partially resolved via scaling solutions. Assuming that the internal basis of the metric relations of proteins is hydrophobic hydration. we demonstrate a relationship between an expanding group action on hydrophobic amino acid sequences and the fractional spatial scalings of amino acid monomeric mass distances in 25 representative proteins. This empirical relationship is analogous to that resulting from the tessellation of non-Euclidean spaces by discrete groups and suggests a route to physical uniformization of the data of protein dynamics without ad hoc scaling corrections.

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Document Details

Document Type
Technical Report
Publication Date
May 01, 1993
Accession Number
ADA328656

Entities

People

  • Arnold J. Mandell
  • Karen A. Selz

Organizations

  • Institut des Hautes Études Scientifiques

Tags

Communities of Interest

  • Air Platforms
  • C4I

DTIC Thesaurus Topics

  • Amino Acids
  • Chemical Synthesis
  • Chemistry
  • Curvature
  • Diffraction
  • Diffraction Analysis
  • Distortion
  • Dynamics
  • Geometry
  • Hydrophobic Properties
  • Military Research
  • Organic Chemistry
  • Proteins
  • Psychology
  • Sequences
  • Transfer Functions
  • Two Dimensional

Readers

  • Mathematical Modeling and Probability Theory.
  • Molecular and Cellular Biochemistry
  • Theoretical Analysis.

Technology Areas

  • Space