| Malhotra, A. and S. Harvey, A Quantitative Model of the Escherichia coli 16 S RNA in the 30 S Ribosomal Subunit. Journal of Molecular Biology, 1994. 240: p. 308340. |
.... diffraction data on the protein positions [9] Malhotra and Harvey have used an energy minimization technique to produce a set of possible conformations for 16S rRNA; their study, however, depends on electron microscopic studies on the molecule to provide initial information on surface topology [10] . Constraint Satisfaction PROTEAN In our study, we use a constraint satisfaction algorithm called PROTEAN, a program originally created to calculate protein structure from constraints derived from nuclear magnetic resonance (NMR) data [11, 12] PROTEAN uses a simplified representation of the ....
.... corresponds closely to a cleft in the topology of the 16S rRNA that has been determined by electron microscopic (EM) studies [23] The structures produced by Malhotra et al. also have this feature, but their methods used the topology generated by the EM studies as a constraint on the structure [10] . Our study used no prior knowledge of topology, and still produces this cleft without the EM data. In addition to the cleft, other aspects of the 16S rRNA topology were consistently preserved among candidate structures. For example, the general location of residues involved in tRNA binding ....
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Malhotra, A. and S. Harvey, A Quantitative Model of the Escherichia coli 16 S RNA in the 30 S Ribosomal Subunit. Journal of Molecular Biology, 1994. 240: p. 308340.
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