The Molecular and Cellular Mechanisms of Quinone Tanning of Proteins.

Abstract

The tyrosine rich eggshell protein referred to as F4 has been modelled exhaustively both by computer simulation and by physical studies of synthetic peptides. Our conclusion is that the tyrosine rich region of this protein probably forms a left-handed alpha helix. I have established the suggestion, based on the established protein segnonces, that the absence of phenylalanine residues may suggest a role in electron transplant.

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Document Details

Document Type
Technical Report
Publication Date
Jun 01, 1994
Accession Number
ADA303501

Entities

People

  • John S. Cordingley

Organizations

  • University of Wyoming

Tags

Communities of Interest

  • Materials and Manufacturing Processes

DTIC Thesaurus Topics

  • Amino Acids
  • Biology
  • Chemistry
  • Computer Simulations
  • Cysteine
  • Electron Transfer
  • Electrons
  • Energy
  • Energy Transfer
  • Molecular Biology
  • New York
  • Phenylalanine
  • Schistosoma
  • Schistosoma Mansoni
  • Simulations
  • Tryptophan
  • Tyrosine

Fields of Study

  • Biology
  • Chemistry

Readers

  • Computational Modeling and Simulation
  • Molecular and Cellular Biochemistry

Technology Areas

  • Biotechnology
  • Microelectronics