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Characterization of soluble artificial proteins with random sequences

A Yamauchi1, T Yomo, F Tanaka

  • 1Department of Biotechnology, Faculty of Engineering, Osaka University, Suita, Japan.

FEBS Letters
|February 19, 1998
PubMed
Summary

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Two random proteins, RP3-42 and RP3-45, exhibit compact oligomeric structures and low esterase activity, comparable to molten globule states. These findings offer insights into protein evolution and structure-function relationships.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Science

Background:

  • Investigating the properties of random proteins provides insights into the fundamental principles of protein folding and function.
  • Understanding the relationship between protein structure and catalytic activity is crucial for protein engineering and drug discovery.

Purpose of the Study:

  • To characterize the structural and catalytic properties of two soluble random proteins, RP3-42 and RP3-45.
  • To compare the characteristics of these random proteins with native proteins from an evolutionary perspective.

Main Methods:

  • Circular Dichroism (CD) spectroscopy to assess secondary structure.
  • Sedimentation equilibrium and small-angle X-ray scattering (SAXS) to determine oligomeric structure and compactness.

Related Experiment Videos

  • Esterase activity assays using p-nitrophenol as a substrate to quantify catalytic rates.

    • Main Results:

    • RP3-42 and RP3-45, each 141 amino acids long, showed no significant secondary structure via CD spectroscopy.
    • Sedimentation equilibrium and SAXS revealed that both proteins form oligomeric structures and are as compact as molten globules.
    • The random proteins displayed low but distinct esterase activity, with second-order rate constants of 0.78 M⁻¹s⁻¹ for RP3-42 and 1.39 M⁻¹s⁻¹ for RP3-45.

    Conclusions:

    • Random proteins can adopt compact, oligomeric structures resembling molten globules, despite lacking defined secondary structures.
    • These random proteins possess intrinsic, albeit low, catalytic activity, suggesting that some functional promiscuity can arise from random sequences.
    • The study contributes to understanding protein evolution by highlighting potential pathways for the emergence of structure and function.