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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Journal of Molecular...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Journal of Molecular Evolution
Article . 1974 . Peer-reviewed
License: Springer TDM
Data sources: Crossref
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Stereospecificity of the genetic code

Authors: G, Melcher;

Stereospecificity of the genetic code

Abstract

A sterical correlation of the amino acids to their anticodon nucleotides is given. The main principle is the intercalation of the amino acid and the binding of the aliphatic amino acid hydrogen atoms through hydrogen bonds to the π-electrons of the bases. The amino groups of the bases and the ribose phosphate chain are additional binding sites for the amino acid. The strength of these hydrogen-π bonds is considerably increased by the protonation of the carboxyl group of the amino acid. Such a protonation occurs in esterification processes and gives in these reactions the possibility of an activated complex where the proposed complementarity is also energetically favoured. Evolutionary considerations show an uncomplicated way from the chemical reactions of prebiologically formed organic molecules to a living system.

Keywords

Binding Sites, Magnetic Resonance Spectroscopy, Base Sequence, Protein Conformation, Molecular Conformation, Biological Evolution, Models, Structural, RNA, Transfer, Genetic Code, Nucleic Acid Conformation, Amino Acid Sequence, Amino Acids, Trichloroacetic Acid, Protein Binding

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    influence
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
35
Top 10%
Top 10%
Average
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