Structural requirements for a primitive adaptor molecule.

G Raghunathan; R Rein

doi:10.1080/07391102.1987.10507696

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Structural requirements for a primitive adaptor molecule.

G Raghunathan·R Rein

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Abstract

Adaptor properties of linear hairpin helices have been examined. The analysis suggests that neither right nor left handed hairpin helices can simultaneously read a comma free messenger and align aminoacyl residues for peptide condensation. Comparison of these studies with the model of the present day peptidyl transfer intermediate suggests that the "L" shaped folding of the present day tRNAs may be a prerequisite for adaptor function. Therefore, the three-dimensional organization of the ancestral adaptor molecule must have had structural features similar to its present day counterpart.

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Amino Acids Anticodon Codon Genetic Code Models, Molecular Nucleic Acid Conformation Peptide Chain Elongation, Translational Protein Biosynthesis RNA, Messenger RNA, Transfer Structure-Activity Relationship Journal Article Research Support, U.S. Gov't, Non-P.H.S.

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G Raghunathan, R Rein. 1987. Structural requirements for a primitive adaptor molecule.. https://doi.org/10.1080/07391102.1987.10507696

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