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Protein structure and function at low temperatures.

R Jaenicke1

  • 1Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, F.R.G.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|January 30, 1990
PubMed
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Proteins adapt to extreme temperatures through subtle amino acid changes, maintaining function. These molecular adaptations involve adjusting protein flexibility via ion pairs and hydrophobic interactions for stability.

Area of Science:

  • Biochemistry and Molecular Biology
  • Evolutionary Biology
  • Biophysics

Background:

  • Proteins are essential cellular components governing organization and metabolism.
  • Organisms adapt to environmental extremes (temperature, pH, water activity), with low-temperature adaptation impacting protein structure, stability, and folding.
  • Protein sequences and topologies across psychrophilic, mesophilic, and thermophilic organisms show high homology.

Purpose of the Study:

  • To investigate the molecular mechanisms of protein adaptation to extreme temperatures.
  • To understand how proteins maintain structure and function under varying thermal conditions.
  • To correlate amino acid sequence alterations with changes in protein stability and free energy.

Main Methods:

  • Comparative analysis of protein sequences and topologies from organisms with different temperature optima.

Related Experiment Videos

  • Statistical and structural analyses of protein interactions and packing density.
  • Investigation of the role of ion pairs and hydrophobic interactions in protein flexibility and stability.

    • Main Results:

    • Adaptive changes in proteins involve multiple amino acid sequence alterations, but specific correlations with structure and stability are not yet fully established.
    • Protein stability is limited at both high and low temperatures.
    • Molecular adaptation to temperature extremes appears to involve a flattening of the temperature profile of the free energy of stabilization.
    • Marginal alterations in intermolecular interactions and packing density are sufficient for adaptation to extreme conditions.

    Conclusions:

    • Protein adaptation to extreme temperatures requires only minor modifications to intermolecular interactions and packing density.
    • Adjusting protein flexibility through alterations in ion pairs and hydrophobic interactions is key to maintaining catalytic function across temperatures.
    • Understanding these molecular adaptations is crucial for comprehending life's resilience in diverse thermal environments.