Multi-Enzyme Complexes in the Thermophilic Archaea: The Effects of Temperature on Stability, Catalysis and Enzyme Interactions in a Multi-Component System

Abstract

Determine the thermostability and thermoactivity of the individual complex components. Study the temperature dependence of whole complex assembly using analytical ultracentrifugation and laser light intensity fluctuation spectroscopy. Investigate the post-translational modification of the E2 component; that is, the lipoylation of the specific lysine in the lipoyl domain. This involves cloning of the genes for the relevant lipoylation enzymes, and characterisation of the protein products.

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Document Details

Document Type
Technical Report
Publication Date
Jan 01, 2012
Accession Number
ADA567244

Entities

People

  • David W. Hough
  • Michael J. Danson

Organizations

  • University of Bath

Tags

Communities of Interest

  • Materials and Manufacturing Processes

DTIC Thesaurus Topics

  • Archaea
  • Assembly
  • Biochemistry
  • Biological Sciences
  • Biology
  • Biotechnology
  • Catalysis
  • Chemistry
  • Electron Spin Resonance
  • Enzymes
  • Intensity
  • Mass Spectrometry
  • Molecular Biology
  • Recombinant Proteins
  • Spectroscopy
  • Spin Resonance
  • Thermostability

Readers

  • Molecular Genetics
  • Molecular and Cellular Biochemistry

Technology Areas

  • Directed Energy