Results 161 to 170 of about 8,979 (206)
Alteration of 5S RNA conformation by ribosomal proteins L18 and L25
Nucleic Acids Research, 1977 The effects of ribosomal proteins L18, L25 and L5 on the conformation of 5S RNA have been studied by circular dichroism and temperature dependent ultraviolet absorbance. The circular dichroism spectrum of native 5S RNA is characterized in the near ultraviolet by a large positive band at 267 nm and a small negative band at 298 nm.
Roger A Garrett +2 more
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rRNA binding domain of yeast ribosomal protein L25
Journal of Molecular Biology, 1991Hendrik A Raue
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Current Genetics, 1987
Using a heterologous probe containing a fragment of the L25-gene from Saccharomyces carlsbergensis we have isolated a DNA-fragment of Candida utilis carrying the gene encoding ribosomal protein L25. This gene is present in a single copy on the C. utilis genome, though as two distinguishable alleles.
Rudi J Planta, L P Woudt, R J Planta
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Using a heterologous probe containing a fragment of the L25-gene from Saccharomyces carlsbergensis we have isolated a DNA-fragment of Candida utilis carrying the gene encoding ribosomal protein L25. This gene is present in a single copy on the C. utilis genome, though as two distinguishable alleles.
Rudi J Planta, L P Woudt, R J Planta
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The Primary Structure of the 5S rRNA Binding Protein L25 of Escherichia coli Ribosomes
Hoppe-Seyler's Zeitschrift Für Physiologische Chemie, 1975The primary structure of protein L25 from the large subunit of Escherichia coli ribosomes was determined by isolation and analysis of peptides obtained after cleavage of the protein with trypsin, thermolysin and Staphylococcus protease as well as by Edman degradation of the intact protein and of a CNBr peptide. The complete amino acid sequence is shown
B Wittmann-Liebold, K G Bitar
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2023
The Minor Planet Electronic Circulars contain information on unusual minor planets, routine data on comets and natural satellites, and occasional editorial announcements. They are published on behalf of Division F of the International Astronomical Union by the Minor Planet Center, Smithsonian Astrophysical Observatory, Cambridge, MA 02138, U.S.A.
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The Minor Planet Electronic Circulars contain information on unusual minor planets, routine data on comets and natural satellites, and occasional editorial announcements. They are published on behalf of Division F of the International Astronomical Union by the Minor Planet Center, Smithsonian Astrophysical Observatory, Cambridge, MA 02138, U.S.A.
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L25 functions as a conserved ribosomal docking site shared by nascent chain‐associated complex and signal‐recognition particle [PDF]
EMBO Reports, 2006 The nascent chain-associated complex (NAC) is a dimeric protein complex of archaea and eukarya that interacts with ribosomes and translating polypeptide chains. We show that, in yeast, NAC and the signal-recognition particle (SRP) share the universally conserved ribosomal protein L25 as a docking site, which is in close proximity to the ribosomal exit ...
Andreas Bracher +2 more
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Thyroid uptake measurement using iodine-l25 and iodine-l31
Physics in Medicine & Biology, 1969Due to the low energy (27.4 kev) of the photons emitted by 125I, the external measurement of thyroid activity requires a significant correction for tissue absorption. This correction can be determined by administering simultaneously a low dose of 131I.
null P Espinasse +2 more
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Current Genetics, 1986
When the gene dosage for the primary rRNA-binding ribosomal protein L25 in yeast cells was raised about 50-fold, the level of mature L25 transcripts was found to increase almost proportionally. The plasmid-derived L25 transcripts were structurally indistinguishable from their genomic counterparts, freely entered polysomes in vivo and were fully ...
Hendrik A Raue, Rudi J Planta, W H Mager
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When the gene dosage for the primary rRNA-binding ribosomal protein L25 in yeast cells was raised about 50-fold, the level of mature L25 transcripts was found to increase almost proportionally. The plasmid-derived L25 transcripts were structurally indistinguishable from their genomic counterparts, freely entered polysomes in vivo and were fully ...
Hendrik A Raue, Rudi J Planta, W H Mager
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Alloy Digest, 2002
Abstract Wieland-L25 is a copper-nickel alloy used almost exclusively as a coining alloy. It shows little variation in its electrical conductivity. This datasheet provides information on composition, physical properties, hardness, and elasticity as well as deformation.
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Abstract Wieland-L25 is a copper-nickel alloy used almost exclusively as a coining alloy. It shows little variation in its electrical conductivity. This datasheet provides information on composition, physical properties, hardness, and elasticity as well as deformation.
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