Predictions for secondary structures of six proteins from the 50 S subunit of the <i>Escherichia coli</i> ribosome

Wittmann‐Liebold, Brigitte; Robinson, S.M.L.; Dzionara, M.

doi:10.1016/0014-5793(77)80959-9

Cited by 23 publications

(5 citation statements)

References 30 publications

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“…The circular dichroism spectra revealed a high content of the α‐helical structure (55–60%) and about 20% of the β‐structure in the L7/L12 dimer [15, 19, 20]. These results are in general agreement with theoretical evaluations of the secondary structure in the protein [21, 22].…”

Section: Structural Studies Of the L7/l12 Proteinsupporting

confidence: 84%

The L7/L12 ribosomal domain of the ribosome: structural and functional studies

Gudkov

1997

FEBS Letters

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The L7/L12 protein forms a functionally important domain in the ribosome. This domain is involved in interaction with translation factors during protein biosynthesis. The tertiary and quaternary structure of the L7/L12 protein was established as a result of intensive studies in solution and in the ribosome. The conformational changes of L7/L12, the elongation factors Tu and G and other ribosomal proteins were traced by different experimental techniques. These changes occur upon interaction of the ribosome with the elongation factors and depend on GTP hydrolysis in accordance with the functional states of the ribosome.

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Section: Structural Studies Of the L7/l12 Proteinsupporting

confidence: 84%

The L7/L12 ribosomal domain of the ribosome: structural and functional studies

Gudkov

1997

FEBS Letters

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“…The secondary structure was predicted using computer programmes based on four different methods [46][47][48]. According to these calculations protein L11 contains about 34-37% a-helical regions, 11-14% /~-structure, and 17-22% turns (or loops).…”

Section: Resultsmentioning

confidence: 99%

The primary structure of L11, the most heavily methylated protein from Escherichia coli ribosomes

Dognin

Wittmann‐Liebold

1977

FEBS Letters

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“…Detailed analyses of circular dichroism data as well as other spectroscopic properties of protein L7/L12 obtained under functionally relevant conditions are not yet available. Pre-0006-2960/79/0418-2019S01.00/0 © 1979 American Chemical Society dictions of secondary structure for L7/L12 that appear in the literature are based entirely on the information available in the amino acid sequence and suggest a-helical content varying from 42 to 64% depending upon the method used (Ptitsyn et al, 1973;Wittmann-Liebold et al, 1977). No /3 structure is evident from either prediction.…”

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confidence: 99%

Conformation of Escherichia coli ribosomal protein L7/L12 in solution: hydrodynamic, spectroscopic, and conformation prediction studies

Luer¹,

Wong²

1979

Biochemistry

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The conformation of Escherichia coli ribosomal protein L7/L12 in solution has been studied using spectroscopic and hydrodynamic methods. Circular dichroism studies in the near-ultraviolet region reveal two bands at 262 and 268 nm originating from the tertiary conformational environment of the phenylalanyl residues. Additional characterization of the phenylalanine environment includes an intrinsic fluorescence emission spectrum arising from the phenylalanine fluorophores. Computer analysis of the far-ultraviolet circular dichroism spectrum suggests that L7/L12 contains as much as approximately 76% alpha helix. Hydrodynamic properties of L7/L12, measured with the purpose of providing relevant shape information, include the frictional coefficient ratio (1.84 +/- 0.03) and intrinsic viscosity (28 +/- 0.4 mL/g). The experimentally determined frictional coefficient (6.15 +/- 0.15 X 10(-8) has been compared with theoretical calculations of the same value employing two independent methods and assuming various dimensions for the L7/L12 dimer. Combining the experimental results from this work with those available from the literature, and using conformation predictive methods of Chou & Fasman [P. Y. Chou & G. D. Fasman (1974) Biochemistry 13, 211-222, 222-245] and of Maxfield & Scheraga (F. R. Maxfield & H. A. Scheraga (1976) Biochemistry 15, 5138-5153), several possible molecular models of the L7/L12 dimer have been constructed and critically examined. A model which is consistent with all of the available data is proposed.

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

Cited by 23 publications

References 30 publications

The L7/L12 ribosomal domain of the ribosome: structural and functional studies

The L7/L12 ribosomal domain of the ribosome: structural and functional studies

The primary structure of L11, the most heavily methylated protein from Escherichia coli ribosomes

Conformation of Escherichia coli ribosomal protein L7/L12 in solution: hydrodynamic, spectroscopic, and conformation prediction studies

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