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Title: | The mechanical properties of proteins determine the laws of evolutionary change |
Authors: | Walker, Ilse |
Keywords: | Amino Acid Dna Enzyme Protein Binding Site Chemistry Conformation Environment Evolution Selection, Genetic Genetic Variability Mutation Phenotype Phylogeny Physiology Amino Acids Binding Sites Chemistry Dna Environment Enzymes Evolution Molecular Conformation Mutation Phenotype Phylogeny Proteins Selection (genetics) Variation (genetics) |
Issue Date: | 1979 |
metadata.dc.publisher.journal: | Acta Biotheoretica |
metadata.dc.relation.ispartof: | Volume 28, Número 4, Pags. 239-282 |
Abstract: | The general inorganic nature of traditional selection theory (based on differential growth between any two systems) is pointed out, wherefrom it follows that this theory cannot provide explanations for the characteristics of organic evolution. Specific biophysical aspects enter with the complexity of macro-molecules: vital physical conditions for the perpetuation of the system, irrevocable extinction (= death) and random change leading to novelty, are the result of 'complexity per se'. Further biophysical properties are a direct function of the pathway along which random mutation in nucleic acids is converted into continuous protein - (specifically enzyme) - function, from there into organismic phenotype with fitness components which may, or may not, correspond to identifiable structural units in DNA. The general machine-like properties of enzymes, in that there is no additive relationship between structural (amino acid) composition and functional output, is discussed in more detail. The continuous growth functions of molecular concentrations, directed by enzyme turnover, determine simple laws of growth and morphogenesis in the organic hierarchy and thus of phenotype. Thus, the combined effect of DNA-structure and of environmental parameters (temperature, pressure, pH, etc.) on protein function determines ultimately the actual phenotype and hence, quality and intensity of genotypic selection. © 1979 Leiden University Press. |
metadata.dc.identifier.doi: | 10.1007/BF00048338 |
Appears in Collections: | Artigos |
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