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Related Experiment Videos

Evolution of model proteins on a foldability landscape

S Govindarajan1, R A Goldstein

  • 1Department of Chemistry, University of Michigan, Ann Arbor 48109-1055, USA.

Proteins
|December 31, 1997
PubMed
Summary

Protein evolution under high selective pressure is confined to neutral networks, preserving native structures. Optimizability strongly influences these networks and the evolutionary process.

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Area of Science:

  • Computational biology
  • Evolutionary dynamics
  • Protein folding

Background:

  • Proteins must fold into specific structures to function.
  • Evolutionary processes shape protein structure and function.
  • Understanding protein evolution requires modeling folding and selection.

Purpose of the Study:

  • To model the evolution of simple lattice proteins.
  • To investigate the role of selective pressure on evolutionary trajectories.
  • To analyze the impact of native structure optimizability on neutral networks.

Main Methods:

  • Random walk model in a fitness landscape.
  • Simulation of protein evolution under varying selective pressures.
  • Analysis of evolutionary trajectories and neutral network properties.

Main Results:

  • Higher selective pressure confines evolutionary trajectories to neutral networks.
  • Within neutral networks, native structures are conserved.
  • Evolutionary dynamics exhibit non-self-averaging and non-exponential behavior.
  • Native structure optimizability significantly affects neutral network size.

Conclusions:

  • Selective pressure and optimizability are key determinants of protein evolutionary pathways.
  • Neutral networks play a crucial role in protein evolution by conserving native structures.
  • The nature of evolutionary dynamics is intrinsically linked to the landscape's optimizability.

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