Prediction of the three‐dimensional structure for ribosomal protein L25

Finkelstein, Alan; Kozitsyn, S. A.; Ptitsyn, Oleg B.

doi:10.1016/0014-5793(75)80436-4

Cited by 3 publications

(1 citation statement)

References 8 publications

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“…Therefore, they do not propose it as a general theoretical method of folding but merely as an illustration that a plausible pathway can be suggested for the folding process. Finkelstein, Kozitsyn & Ptitsyn (1975) used this method in a modified form to predict the three-dimensional structure of ribosomal protein L 25. The structure has not been determined experimentally.…”

Section: B Medium-and Long-range Interaction Modelsmentioning

confidence: 99%

Protein folding

Némethy

Scheraga

1977

Quart. Rev. Biophys.

296

125

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This review describes recent advances in studies on the stabilities of the three-dimensional structures of proteins and on the processes leading to the formation of these structures. The term ‘protein folding’ will be used here to denote the process of the conversion of an open polypeptide chain into the unique three-dimensional conformation of the native protein. Experimental and theoretical aspects of protein folding have been reviewed by anfinsen & Scheraga (1975). In the present article, we emphasize advances made since the writing of that review, together with a brief summary of the background of recent studies.

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Section: B Medium-and Long-range Interaction Modelsmentioning

confidence: 99%

Protein folding

Némethy

Scheraga

1977

Quart. Rev. Biophys.

296

125

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Predictions for secondary structures of six proteins from the 50 S subunit of the Escherichia coli ribosome

1977

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Purification and conformation of ribosomal protein L25 from E. coli ribosome

Fox

Owens

Wong

1988

International Journal of Peptide and Protein Research

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Ribosomal protein L25 from the large subunit of E. coli ribosomes has been purified using a new procedure involving a 2 M LiCl extraction followed by phosphocellulose chromatography in 6~ urea elution buffer. The conformation of purified L25 was studied employing circular dichroism and ultraviolet absorption spectroscopy in reconstitution buffer. The analysis of the far U.V. circular dichroism spectrum of L25 indicates L25 contains -16% a-helix and -19% j-structure. The conformation of L25 was also studied using the predictive methods of Chou & Fasman and Maxfield & Scheraga. Both of these methods predict approximately three times the percent a-helix present in L25 as compared with that determined from the analysis of the circular dichroism spectrum. A structure for L25 is predicted which contains two positively charged binding domains and is consistent with published binding data on the interaction of 5 s RNA and L25. The large difference in the % cc-helix as determined from the analysis of the circular dichroism spectrum and the predictive techniques is suggested to result from the denaturing effects of 6~ urea used in the preparation of ribosomal proteins.The ribosomal protein L25 has been identified as one of the three ribosomal proteins (L25, L18, and L5) which bind to 5 s RNA (1-3). Protein L25 exhibits the greatest affinity for 5s RNA. than 5 S RNA alone, indicating a cooperative binding of these proteins t o 5 S RNA (4). This protein, along with L18 and L5, must be present in order for 5 S RNA to attach to core particles of E. coli ribosomes (1). The amino acid sequence of L25 has been determined and found to contain 94 amino acids with a molecular weight of 10912 (5). A threedimensional structure has been predicted for L25 based on its amino acid sequence and the assumption that L25 has a globular shape (6).In order to study the structure of L25 and the structure of the 5s RNA-L25 protein complex, we initially sought a simple procedure in which to purify L25 from the

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Prediction of the three‐dimensional structure for ribosomal protein L25

Cited by 3 publications

References 8 publications

Protein folding

Protein folding

Predictions for secondary structures of six proteins from the 50 S subunit of the Escherichia coli ribosome

Purification and conformation of ribosomal protein L25 from E. coli ribosome

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