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Buried charged surface in proteins.

T Kajander1, P C Kahn, S H Passila

  • 1Centre for Biotechnology, University of Turku, Turku, Finland.

Structure (London, England : 1993)
|November 18, 2000
PubMed
Summary
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Buried charges in proteins are more common than previously thought, increasing with protein size. This finding suggests charge burial may reduce protein stability and offers new ways to engineer protein thermophilicity.

Area of Science:

  • Protein Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Traditionally, charged amino acids in globular proteins are believed to be primarily on the exterior, exposed to solvent.
  • Buried charges were thought to be rare and primarily involved in critical functions like catalysis, ligand binding, or structural stabilization (e.g., helix caps).

Purpose of the Study:

  • To investigate the prevalence and distribution of buried charges in proteins across various sizes.
  • To determine the relationship between protein size and the amount of buried charge.
  • To explore the functional implications of buried charges on protein stability and thermophilicity.

Main Methods:

  • Analysis of buried charged surface and charge distribution in a wide range of protein sizes.
  • Experimental testing involving site-directed mutagenesis (D178N substitution in muconate lactonizing enzyme).

Related Experiment Videos

  • Free energy calculations to assess protein stability.

    • Main Results:

    • Buried charge is significantly more common in proteins than previously assumed.
    • The proportion of buried charge increases with protein size, distinct from other surface types.
    • In large proteins like hemocyanin, a substantial percentage (35%) of charges are highly buried (>75%).
    • Experimental mutation of a buried charge (D178N) stabilized the enzyme by 4.2°C without altering its structure.
    • Free energy calculations corroborated the experimental findings on stability.

    Conclusions:

    • Protein charge burial may serve as a mechanism to modulate protein stability, potentially reducing it.
    • Not all buried charges are inherently stabilized by their surrounding protein environment.
    • Thermophilic proteins generally exhibit less buried charge.
    • Targeted modification of buried charges presents a viable strategy for engineering protein thermophilicity or psychrophilicity.