Water, Protein Folding, and the Genetic Code
- 2 November 1979
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 206 (4418), 575-577
- https://doi.org/10.1126/science.493962
Abstract
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.Keywords
This publication has 12 references indexed in Scilit:
- Interaction of the peptide bond with solvent water: a vapor phase analysisBiochemistry, 1978
- The nature of the accessible and buried surfaces in proteinsJournal of Molecular Biology, 1976
- Structural effects on rates and equilibriums. XIX. Intrinsic hydrophilic character of organic compounds. Correlations in terms of structural contributionsThe Journal of Organic Chemistry, 1975
- The interpretation of protein structures: Estimation of static accessibilityJournal of Molecular Biology, 1971
- Models for the evolution of codon assignmentsJournal of Molecular Biology, 1969
- The origin of the genetic codeJournal of Molecular Biology, 1968
- Structure and function of haemoglobinJournal of Molecular Biology, 1965
- On the Coding of Genetic InformationCold Spring Harbor Symposia on Quantitative Biology, 1963
- Volume Changes in Protein Reactions. II. Comparison of Ionization Reactions in Proteins and Small MoleculesJournal of the American Chemical Society, 1962
- The energy and entropy of hydration of organic compoundsTransactions of the Faraday Society, 1937