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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
A structural model of latent evolutionary potentials underlying neutral networks in proteins
HFSP Journal
|May 1, 2009
Summary
Neutral mutations can facilitate protein adaptation by enabling smooth phenotypic transitions. This occurs through near-ground-state protein structures, allowing latent traits to adapt before gene duplication.
Area of Science:
- Molecular Evolution
- Protein Biophysics
- Biochemistry
Background:
- Understanding protein adaptability to new requirements is a central question in molecular evolution.
- Proteins fluctuate between structures, with frequencies related to stability, suggesting functional promiscuity.
- Near-ground-state structures may represent multiple selectable traits and facilitate phenotypic transitions.
Purpose of the Study:
- To investigate if neutral mutations facilitate or hinder protein adaptability.
- To explore the role of near-ground-state protein structures in enabling smooth phenotypic transitions.
- To provide a biophysical explanation for experimental observations of adaptation via neutral mutations.
Main Methods:
- Utilized a biophysical heteropolymer model.
- Performed exhaustive mappings of protein sequences to structures.
- Analyzed stability gradients and mutational proximity in genotype space.
Main Results:
- Demonstrated that near-ground-state structures facilitate smooth phenotypic transitions.
- Showed optimization of structural phenotypes is possible along a smooth stability gradient.
- Confirmed mutational proximity of similar phenotypes in genotype space.
Conclusions:
- Near-ground-state structures enable adaptation to new requirements while maintaining existing functions.
- Pleiotropy, facilitated by neutral mutations, aids adaptation of latent traits before gene duplication.
- This mechanism enhances the effective adaptability of proteins.
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