title: Structural requirements for a primitive adaptor molecule.
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.
authors.affiliation: Department of Biophysics, Roswell Park Memorial Institute, Buffalo, New York 14263.
authors.forename: G
authors.initials: G
authors.lastname: Raghunathan
authors.forename: R
authors.initials: R
authors.lastname: Rein
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D000926:Anticodon / Q000648:ultrastructure; D003062:Codon / Q000648:ultrastructure; D005815:Genetic Code; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D010441:Peptide Chain Elongation, Translational; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000648:ultrastructure; D012343:RNA, Transfer / Q000648:ultrastructure*; D013329:Structure-Activity Relationship
chemical_list: D000596:Amino Acids; D000926:Anticodon; D003062:Codon; D012333:RNA, Messenger; D012343:RNA, Transfer