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Related Experiment Videos

Truncated staphylococcal nuclease is compact but disordered.

J M Flanagan1, M Kataoka, D Shortle

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.

Proceedings of the National Academy of Sciences of the United States of America
|January 15, 1992
PubMed
Summary

A truncated staphylococcal nuclease lacking secondary structure remains compact and active. This protein folding study suggests solvent exclusion drives early protein compactness during biosynthesis.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Folding

Background:

  • Staphylococcal nuclease (SN) is a model protein for studying folding.
  • Carboxyl-terminal deletions can yield partially unfolded protein states.

Purpose of the Study:

  • To characterize a staphylococcal nuclease mutant with a 13-amino acid carboxyl-terminal deletion.
  • To investigate the folding behavior and structural properties of this truncated protein.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy
  • Circular dichroism (CD) spectroscopy
  • Small-angle X-ray scattering (SAXS)

Main Results:

  • The truncated nuclease is compact but lacks persistent secondary structure.

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  • It retains wild-type enzymatic activity in the presence of calcium.
  • The molecule folds into a native-like conformation upon binding a potent inhibitor (3',5'-bisphospho-2'-deoxythymidine).

    • Conclusions:

    • The truncated staphylococcal nuclease retains the capacity for folding.
    • Results suggest solvent exclusion is a key factor in generating compact polypeptide structures during early stages of protein biosynthesis, preceding secondary structure formation.