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A relationship between protein stability and protein function

B K Shoichet1, W A Baase, R Kuroki

  • 1Institute of Molecular Biology, Howard Hughes Medical Institute, University of Oregon, Eugene 97403.

Proceedings of the National Academy of Sciences of the United States of America
|January 17, 1995
PubMed
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Mutating key sites in T4 lysozyme enhanced protein stability but reduced enzymatic activity. This suggests a trade-off between enzyme function and thermal stability.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Enzymes rely on ordered structures for catalysis.
  • A prevailing hypothesis suggests that functionally critical enzyme residues are not optimized for stability.

Purpose of the Study:

  • To investigate the relationship between enzyme function and stability.
  • To test the hypothesis that functionally important residues are not optimized for stability using T4 lysozyme.

Main Methods:

  • Site-directed mutagenesis of catalytically important (Glu-11, Asp-20) and substrate-binding (Ser-117, Asn-132) residues in T4 lysozyme.
  • Assays to measure enzymatic activity and thermal stability.
  • X-ray crystallography to determine structural changes.

Related Experiment Videos

Main Results:

  • Mutations at catalytic residues reduced activity but increased stability by 0.7-1.7 kcal/mol.
  • Mutations at substrate-binding residues increased stability by 1.2-2.0 kcal/mol, also decreasing activity.
  • X-ray structures revealed complementary surface interactions and conformational changes upon mutation.

Conclusions:

  • Results support a functional trade-off between stability and activity in T4 lysozyme.
  • The findings suggest a general relationship between enzyme stability and function.