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Protein structure and neutral theory of evolution.

O B Ptitsyn1, M V Volkenstein

  • 1Institute of Protein Research Academy of Sciences of the USSR, Pushchino, Moscow Region.

Journal of Biomolecular Structure & Dynamics
|August 1, 1986
PubMed
Summary

Protein evolution may involve random sequences edited by natural selection. Many protein structures arise from inherent physical properties, not just strategic sequence selection.

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Area of Science:

  • Evolutionary Biology
  • Biochemistry
  • Protein Science

Background:

  • The neutral theory of evolution explains genetic drift's role in molecular evolution.
  • Understanding protein origins requires integrating evolutionary theory with biophysical principles.

Purpose of the Study:

  • To extend the neutral theory of evolution to the origin of protein molecules.
  • To investigate the role of random sequences and physical constraints in protein structure formation.

Main Methods:

  • Formulation of physical requirements for functional globular proteins.
  • Analysis of amino acid sequences, including random sequences, for structural properties.
  • Comparison of structural features in random sequences versus real proteins.

Main Results:

  • Many globular protein sequences may be 'memorized' random sequences, with evolution acting as an 'editor'.
  • Physical requirements for protein structure, like alpha-helices and beta-strands, are inherent in random sequences.
  • Random sequences can form 3D folding patterns similar to real proteins, suggesting limited need for strong selection on overall structure.

Conclusions:

  • Biological selection is primarily crucial for creating protein active sites and ensuring stability under physiological conditions.
  • Protein structure and function may arise from a combination of random sequence generation and targeted evolutionary editing.
  • The neutral theory provides a framework for understanding the non-adaptive aspects of protein evolution.

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