Evolution of protein cores: Constraints in point mutations as observed in globin tertiary structures

摘要: Abstract The amino acid sequences of ten globin chain tertiary structures were aligned and structurally equivalenced by spatial superposition main-chain Cα atoms. A search was then performed for equivalent residue pairs that buried in the protein core had mutated but maintained similar unmutated environments. Residues with atoms contact such central define their Such examples point mutations would represent vivo site-directed mutagenesis as be observed evolution. exposed residues also performed. constraints placed on characteristics (e.g., side-chain volume, polarity, radius gyration) allow suggestions evolutionary modes surface development well substitution guidelines to maintain structural stability engineering design.