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Protein structure and neutral theory of evolution.
1Institute of Protein Research Academy of Sciences of the USSR, Pushchino, Moscow Region.
Journal of Biomolecular Structure & Dynamics
|August 1, 1986
Summary
Protein evolution may involve random sequences edited by natural selection. Many protein structures arise from inherent physical properties, not just strategic sequence selection.
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.