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The Genetic Control of Tertiary Protein Structure: Studies With Model Systems
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References
1963
Year
Structural BioinformaticsBiomolecular Structure PredictionGeneticsProtein AnalysisMolecular BiologyMolecular GeneticsAnalytical UltracentrifugationMembrane ProteinsProtein FoldingTertiary Protein StructureComputational BiochemistryMacromolecular AssembliesThree-dimensional ConfigurationBiochemistryDirected EvolutionTertiary StructureProtein ModelingProtein Structure PredictionStructural BiologyBiomolecular EngineeringGenetic ControlNatural SciencesComputational BiologyModel SystemsProtein EvolutionConfigurational SpecificityMolecular BiophysicsSystems BiologyMedicine
At the present time it is generally assumed that most, if not all, proteins possess well-defined structures. This assumption is based on several kinds of evidence: (1) the finding that many proteins have unique amino acid sequences, with specific intrachain disulfide bonds; (2) the ability to determine the three-dimensional configuration (tertiary structure) and, in some instances, even portions of the amino acid sequence of proteins such as myoglobin and hemoglobin by X-ray crystallographic methods; (3) the highly reproducible physical-chemical properties of a large number of proteins; and (4) the great degree of configurational specificity which appears necessary for enzymic activity. When one considers the complexity of the tertiary structure of a “native” protein, it seems reasonable to inquire into how a newly-made protein arrives at its three-dimensional configuration.