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Fundamentals of protein stability
Fundamentals of protein stability

... The frontiers of viability of living organisms are marked by extreme conditions: 1 12 for pH, -5 110°C for temperature, 0.1 120 MPa for hydrostatic pressure, and 0.6 1.0 for water activity. While organisms existing at extreme pH usually maintain neutral pH in their cytoplasm by active proton pumps, ...
RNA and Protein Synthesis
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Proteomic Mapping of Mitochondria in Living Cells
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Section 5.3: Proteins
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Additional file 11 cd00120: MCM1, Agamous, Deficiens, and SRF
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PDF Copy - Brandon S. Russell, Ph.D.
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... does not noticeably perturb cellular function. Using extensive control experiments, they also demonstrated that translation with Aha is specific only for proteins synthesized after the introduction of Aha, and that its incorporation does not alter global protein synthesis kinetics. This highlights o ...
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... DTL was recovered through its interaction with a mammalian virus RNA. This is why to characterize mammalian homologue of DTL might support and clarify certain aspects of DTL. Since the amino acid similarities shared by DTL and its relatives were located in the C-terminal half of the homologues, a mu ...
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... An incomplete protein can be combined with another meat or plant proteins to be upgraded to a complete protein What is a limiting amino acid? An amino acid that is in the shortest supply in an incomplete protein What are complemented proteins? Do they have to eaten at the same time? Incomplete prote ...
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... E-mail: [email protected] ...
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Amino acid sequence restriction in relation to proteolysis
Amino acid sequence restriction in relation to proteolysis

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protein - Warren County Schools
protein - Warren County Schools

... Transcription is done…what now? Now we have mature mRNA transcribed from the cell’s DNA. It is leaving the nucleus through a nuclear pore. Once in the cytoplasm, it finds a ribosome so that translation can begin. ...
What are proteins - Assiut University
What are proteins - Assiut University

... Some proteins are composed of more than one polypeptide chain. Each polypeptide chain is called a subunit. For example, if a protein is composed of two polypeptides, then it has two subunits. The polypeptides may or may not be different in primary structure. ...
Powerpoint slides
Powerpoint slides

... • Transcription of the mRNA that codes for the protein from DNA in the nucleus. • Export of the mRNA from the nucleus through pores in the nuclear envelope. • Translation of the mRNA on ribosomes on rough Endoplasmic Reticulum (ER) to make the protein. •The protein is threaded into the lumen of the ...
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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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