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Protein Synthesis and Degradation
Protein Synthesis and Degradation

... map. The core of the interface between the 30S small subunit and the 50S large subunit, where the tRNA substrates are bound, is dominated by RNA, with proteins located mainly at the periphery, consistent with ribosomal function being based on rRNA. In each of the three tRNA binding sites, the riboso ...
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What is a protein?

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chapter3_Sections 4
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Voice E. coli Expression System Efficiently Secretes Recombinant
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... protein product with its natural N-terminus. In a second step of synthesis, correctly folded proteins are released from bacterial periplasmic spaces into the culture broth. This step is mediated by a unique feature of the proprietary WCM105 strain, which has a modified outer membrane for efficient s ...
Plant serine/arginine-rich proteins and their role in pre
Plant serine/arginine-rich proteins and their role in pre

... one of these proteins (UBP) in protoplasts enhanced the splicing of pre-mRNAs that are otherwise inefficiently processed. The importance of the GC content in exons in efficient splicing, and an AG-rich exonic element in promoting downstream 5 0 splice site selection, has also been reported in some c ...
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Protein-Protein Interactions
Protein-Protein Interactions

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... Fibrous proteins are found in hair, fingernails, animal claws and fur among other things. These proteins are strong because the individual protein molecules form parallel strands which twist together. Globular protein molecules work differently. A globular molecule twists and folds upon itself, usin ...
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... RNA polymerase RNA processing RNA splicing signal peptide signal-recognition particle (SRP) spliceosome TATA box template strand terminator transcription transcription factor transcription initiation complex transcription unit transfer RNA (tRNA) translation triplet code wobble Word Roots anti- 5 op ...
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Biochem  Fall 2011 Sample Exam I – Protein Structure
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Protein–protein interactions
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Lecture_3. ppt - Department of Molecular & Cell Biology
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... Transfer proteins to membranes (i.e. Nitrocellulose) Block non-specific sites on membrane Incubate with primary antibody, wash Incubate with secondary antibody, wash Detect secondary antibody ...
Chapter 1. Introduction 1. Introduction 1.1 Peptidyl
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The Unfolded Protein Response in C. Elegans
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... The observed deficiency in UPR, could lie in ire-1 since this gene codes for the endonuclease that signals ER stress by splicing (and activating) the mRNA for Xbp-1. Xbp-1 is a transcription factor, which activates the hsp-4 and other genes, required for the UPR. We are currently attempting to deter ...
Protein Structures - the University of California, Davis
Protein Structures - the University of California, Davis

... http://www.ebi.ac.uk/thornton-srv/software/PROCHECK/ -Or through the PDBsum web portal: http://www.ebi.ac.uk/pdbsum/ ...
Protein Structures: Experiments and Modeling
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... http://www.ebi.ac.uk/thornton-srv/software/PROCHECK/ -Or through the PDBsum web portal: http://www.ebi.ac.uk/pdbsum/ ...
DNA Replication - Texas Tech University
DNA Replication - Texas Tech University

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ap® biology 2009 scoring guidelines - AP Central
ap® biology 2009 scoring guidelines - AP Central

... “[I]t undergoes RNA splicing by the spliceosomes. These enzymes cut out the intron.” “Ribosomes are where proteins are made.” “When tRNA attaches, it brings with it an amino acid.” The maximum of 4 points were earned in part (b). Acetylation and methylation are the mechanisms of protein regulation n ...
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Solubility of proteins
Solubility of proteins

... (From ExPASy Biochemical Pathways; http://www.expasy.org/cgi-bin/show_thumbnails.pl?2) ...
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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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