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Rationalization of some genetic anticodonic assignmentsThe hydrophobicity of most amino acids correlates well with that of their anticodon nucleotides, with Trp, Tyr, Ile, and Ser being the exceptions to this rule. Using previous data on hydrophobicity and binding constants, and new data on rates of esterification of polyadenylic acid with several N-acetylaminoacyl imidazolides, several of the anticodon assignments are rationalized. Chemical reasons are shown supporting the idea of the inclusion of the Ile in the catalog of biological amino acids late in the evolution, through a mutation of the existing tRNA and its aminoacyl-tRNA-synthetase. It was found that an addition of hexane increases the incorporation of hydrophobic Ac-Phe into poly-A, in support of the Fox (1965) and Oparin (1965) emphasis on the biogenetic importance of phase-separated systems.
Document ID
19860043985
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Lacey, J. C., Jr.
(Alabama Univ. Birmingham, AL, United States)
Hall, L. M.
(Alabama Univ. Birmingham, AL, United States)
Mullins, D. W., Jr.
(Alabama, University Birmingham, United States)
Date Acquired
August 12, 2013
Publication Date
January 1, 1985
Publication Information
Publication: Origins of Life
Volume: 16
Issue: 1 19
ISSN: 0302-1688
Subject Category
Space Biology
Accession Number
86A28723
Funding Number(s)
CONTRACT_GRANT: NGR-01-010-001
Distribution Limits
Public
Copyright
Other

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