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Complexes of polyadenylic acid and the methyl esters of amino acidsA study of amino acid methyl esters binding to polyadenylic acid supports the theory that the genetic code originated through weak but selective affinities between amino acids and nucleotides. NMR, insoluble complex analysis, and ultraviolet spectroscopy are used to illustrate a correlation between the hydrophybicities of A amino acids and their binding constants, which, beginning with the largest, are in the order of Phe (having nominally a hydrophobic AAA anticodon), Ile, Leu, Val and Gly (having a hydrophilic anticodon with no A). In general, the binding constants are twice the values by Reuben and Polk (1980) for monomeric AMP, which suggests that polymer amino acids are interacting with only one base. No real differences are found betwen poly A binding for free Phe, Phe methyl ester or Phe amide, except that the amide value is slightly lower.
Document ID
19840040056
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
External Source(s)
Authors
Khaled, M. A.
(Alabama Univ. Birmingham, AL, United States)
Mulins, D. W., Jr.
(Alabama Univ. Birmingham, AL, United States)
Swindle, M.
(Alabama Univ. Birmingham, AL, United States)
Lacey, J. C., Jr.
(Alabama, University Birmingham, AL, United States)
Date Acquired
August 12, 2013
Publication Date
December 1, 1983
Publication Information
Publication: Origins of Life
Volume: 13
ISSN: 0302-1688
Subject Category
Space Biology
Accession Number
84A22843
Funding Number(s)
CONTRACT_GRANT: NGR-01-010-001
Distribution Limits
Public
Copyright
Other

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