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Proteins
Proteins

... The total globulin level in serum is determined by a ...
Phloem RNA-binding proteins as potential components of the long
Phloem RNA-binding proteins as potential components of the long

... of the ribonucleotide complexes that function to regulate RNA transport or metabolism. eIF5A contains a KOW motif (acronym of the authors surname, Kyrpides et al., 1996) characterized by the presence of an invariant glycine residue and five alternating blocks of hydrophilic and hydrophobic residues ( ...
Macromolecules
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... sort of like the 4-helix bundle, but with just two helices. Originally it was thought that the leucyl residues interdigitated (hence the name, "leucine zipper"), but it is now believed that they face each other (reality in the form of x-ray crystallography strikes again). In any case, the symmetric ...
Molecular Biology
Molecular Biology

... • RNA polymerase II (Pol II; also known as RNAP II). It transcribes protein-encoding genes into mRNA (and also the snRNA genes). • RNA polymerase III (Pol III). It transcribes the 5S rRNA genes and all the tRNA genes. ...
Document
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... Chemical Structure of Proteins ◦ Proteins are built from amino acids held together by peptide bonds. The amino acids confer shape and properties to the protein. ◦ Two or more polypeptide chains may associate to form a protein complex. Each cell type has characteristic proteins associated with its fu ...
The orphan histidine protein kinase SgmT is a cdiGMP receptor and
The orphan histidine protein kinase SgmT is a cdiGMP receptor and

... A fundamental property of bacterial cells is their ability to respond to changes in the extracellular and intracellular environments. In this context, specific inputs are coupled to specific outputs by dynamically interacting signalling proteins organized in regulatory pathways. In order to ensure a ...
RNA Polymerase - California Lutheran University
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lecture1.pps
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...  While proteins that have little to do with each other in the cells, their genes are adjacent  Therefore, in brief decoding genomes is not a simple matter  Even with the aid of powerful computers, it is still difficult for researchers • to locate definitively the beginning and end of genes in the ...
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... Using 2-D liquid separation and an ESI-TOF MS-based mass mapping technique, we examined the differences in the proteomic profiles of the permafrost bacterium E. sibiricum 255-15 grown at two temperatures (4oC and 25oC) and two media (liquid broth and agar surface) before freeze-thawing treatments. I ...
Polymer scaling laws of unfolded and intrinsically disordered
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... enough to determine ρ0 independently, we fixed lp  (but not ρ0 ) to this value of 0.40 nm. For comparison, a free fit of the length scaling of RG for 10,905 folded proteins selected from the Protein Data Bank results in ν ¼ 0.34 and a persistence length of lp  ¼ 0.53 nm (Fig. 2) (35), but even usi ...
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... enough to determine ρ0 independently, we fixed lp  (but not ρ0 ) to this value of 0.40 nm. For comparison, a free fit of the length scaling of RG for 10,905 folded proteins selected from the Protein Data Bank results in ν ¼ 0.34 and a persistence length of lp  ¼ 0.53 nm (Fig. 2) (35), but even usi ...
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sv-lncs - School of Mathematical and Computer Sciences
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... A series of studies attempting to reveal the modules in cellular networks, ranging from metabolic,[5] to protein networks,[6, 7] strongly support the proposal that modular architecture is one of the principles underlying biological organisation. The modular nature of the cellular networks, including ...
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... Many vectors are now engineered with DNA sequences encoding a specific peptide (purification tag) that, when fused to the expressed protein, may be used for one-step purification of the recombinant protein by high-affinity binding. That is molecular biologists design expression systems such that the ...
041118-SusanWong
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... Will provide 35 million doses for young people, schoolchildren, women and all those at particular risk through their work. Assist countries in making the transition to self sustained programs. ...
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SR protein



SR proteins are a conserved family of proteins involved in RNA splicing. SR proteins are named because they contain a protein domain with long repeats of serine and arginine amino acid residues, whose standard abbreviations are ""S"" and ""R"" respectively. SR proteins are 50-300 amino acids in length and composed of two domains, the RNA recognition motif (RRM) region and the RS binding domain. SR proteins are more commonly found in the nucleus than the cytoplasm, but several SR proteins are known to shuttle between the nucleus and the cytoplasm.SR proteins were discovered in the 1990s in Drosophila and in amphibian oocytes, and later in humans. In general, metazoans appear to have SR proteins and unicellular organisms lack SR proteins.SR proteins are important in constitutive and alternative pre-mRNA splicing, mRNA export, genome stabilization, nonsense-mediated decay, and translation. SR proteins alternatively splice pre-mRNA by preferentially selecting different splice sites on the pre-mRNA strands to create multiple mRNA transcripts from one pre-mRNA transcript. Once splicing is complete the SR protein may or may not remain attached to help shuttle the mRNA strand out of the nucleus. As RNA Polymerase II is transcribing DNA into RNA, SR proteins attach to newly made pre-mRNA to prevent the pre-mRNA from binding to the coding DNA strand to increase genome stabilization. Topoisomerase I and SR proteins also interact to increase genome stabilization. SR proteins can control the concentrations of specific mRNA that is successfully translated into protein by selecting for nonsense-mediated decay codons during alternative splicing. SR proteins can alternatively splice NMD codons into its own mRNA transcript to auto-regulate the concentration of SR proteins. Through the mTOR pathway and interactions with polyribosomes, SR proteins can increase translation of mRNA.Ataxia telangiectasia, neurofibromatosis type 1, several cancers, HIV-1, and spinal muscular atrophy have all been linked to alternative splicing by SR proteins.
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