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PubMed · 14995643

Sequence variability of proteins evolutionarily constrained by solution-thermodynamic function.

F N Braun
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Abstract

Focusing on silk fibroin and hemoglobin molecules as templates, we model protein homolog dispersal across sequence-fitness landscapes determined by solution thermodynamics. Landscapes are constructed by inspecting an idealized theoretical phase topology associated with sequence length and hydrophobic-polar composition, comprising liquid-liquid phase separation, gelation and liquid crystalline self-assembly. We then calculate the distribution of homologs in sequence space as steady states of a simple mutation-selection dynamics. The results are consistent with Swiss-Prot bioinformatic data.

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Amino Acid SequenceComputer SimulationDimerizationEvolution, MolecularFibroinsGenetic VariationHemoglobinsInsect ProteinsModels, ChemicalModels, GeneticMolecular Sequence DataPhylogenyProtein BindingProteinsSequence Analysis, ProteinSequence Homology, Amino AcidSilkSolutionsStructure-Activity RelationshipThermodynamicsJournal ArticleResearch Support, Non-U.S. Gov't

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F N Braun. 2004-01-16. Sequence variability of proteins evolutionarily constrained by solution-thermodynamic function.. https://doi.org/10.1103/physreve.69.011903

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