The solution structure of transfer RNA studied by proton NMR
The adaptor role of transfer RNA in protein biosynthesis was discovered some twenty years ago (Hoagland et al., 1957). Fifteen years ago the nucleotide sequence of the first tRNA molecule was determined by Holley and coworkers (Holley et al., 1965). The primary sequence led to the prediction of the well-known cloverleaf secondary structure which has been amply corroborated by the determination of over 80 tRNA sequences in the last ten years (Sprinzl et al., 1978). Elucidation of higher order folding into a defined three-dimensional structure was complicated by the difficulty in obtaining well-ordered crystals of this highly charged polymer. Six years ago Kim and Rich and coworkers at M.I.T. (Kim et al., 1974) and the Klug group at M.R.C. Cambridge (Robertus et al., 1974) reported the tertiary interactions in the crystal structure of yeast tRNAPhe at intermediate crystallographic resolution. The high-resolution refined structure has been reported by four laboratories (Jack et al., 1976; Quigley et al., 1975; Stout et al., 1978; Sussman et al., 1978); the three-dimensional folding and tertiary interactions are in virtually complete agreement in these four refined structures and are discussed in detail in chapter 5.
KeywordsMagnesium Cobalt Adenosine Adenine Phenylalanine
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