The primary structure of human ribosomal protein L12

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The primary structure of human ribosomal protein L12.

The ribosome serves as the site of protein synthesis in all cells. Biogenesis of the mammalian ribosome is a complex process involving the coordinated expression of four ribosomal RNA molecules and approximately 75 ribosomal proteins. In order to understand the mechanisms governing ribosome biosynthesis, it is necessary to elucidate the structure and organization of its components. A cDNA clone...

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High Level Expression of Recombinant Ribosomal Protein (L7/L12) from Brucella abortus and Its Reaction with Infected Human Sera

Brucellosis, caused by Brucella spp., is an important zoonotic disease that causes abortion and infertility in cattle and undulant fever in humans. Various studies have examined cell-free native and recombinant proteins as candidate protective antigens in animal models. Among Brucella immunogenes, antigen based on ribosomal preparation has been widely investigated. In this study, the immunogeni...

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Immunogencity of HSA-L7/L12 (Brucella abortus Ribosomal Protein) in an Animal Model

Background: The immunogenic Brucella abortus ribosomal protein L7/L12 is a promising candidate antigen for the development of subunit vaccines against brucellosis. Objective: This study was aimed to evaluate the protection of recombinant Human Serum Albumin (HAS)-L7/L12 fusion protein in Balb/c mice. Methods: The amplified L7/L12 gene was cloned in pYHSA5 vector, pYHSA5-L7/L12 construct was tra...

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Expression of human serum albumin--L7/L12 (Brucella abortus ribosomal protein) fusion protein in Saccharomyces cerevisiae.

Brucella abortus is a facultative intracellular gram-negative bacterial pathogen that causes abortion in pregnant cattle and undulant fever in humans. The immunogenic B. abortus ribosomal protein L7/L12 is a promising candidate antigen for the development of subunit vaccines against brucellosis. It has already been expressed in several bacteria and has been used as DNA vaccine. In order to cons...

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Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation.

Ribosomal protein L12 is a two-domain protein that forms dimers mediated by its N-terminal domains. A 20-residue linker separates the N- and C-terminal domains. This linker results in a three-lobe topology with significant flexibility, known to be critical for efficient translation. Here we present an ensemble model of spatial distributions and correlation times for the domain reorientations of...

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ژورنال

عنوان ژورنال: Nucleic Acids Research

سال: 1993

ISSN: 0305-1048,1362-4962

DOI: 10.1093/nar/21.3.749