论文信息 - Water, protein folding, and the genetic code. - 字舞流文

Water, protein folding, and the genetic code.

The absolute affinities of amino acid side chains for solvent water closely match their relative distributions between the surface and the interior of native proteins and are associated with a remarkable bias in the genetic code.

R. Wolfenden | P. Cullis | C. C. Southgate

[1] J. Butler. The energy and entropy of hydration of organic compounds , 1937 .

[2] W. Kauzmann,et al. Volume Changes in Protein Reactions. II. Comparison of Ionization Reactions in Proteins and Small Molecules , 1962 .

[3] S. Pestka,et al. On the Coding of Genetic Information , 1963 .

[4] F. Crick. Origin of the Genetic Code , 1967, Nature.

[5] Models for the evolution of codon assignments. , 1969, Journal of molecular biology.

[6] B. Lee,et al. The interpretation of protein structures: estimation of static accessibility. , 1971, Journal of molecular biology.

[7] C. Tanford,et al. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. , 1971, The Journal of biological chemistry.

[8] H. Bull,et al. Surface tension of amino acid solutions: a hydrophobicity scale of the amino acid residues. , 1974, Archives of biochemistry and biophysics.

[9] J. Hine,et al. Structural effects on rates and equilibriums. XIX. Intrinsic hydrophilic character of organic compounds. Correlations in terms of structural contributions , 1975 .

[10] C. Chothia. The nature of the accessible and buried surfaces in proteins. , 1976, Journal of molecular biology.

[11] R. Wolfenden,et al. Interaction of the peptide bond with solvent water: a vapor phase analysis. , 1978, Biochemistry.