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RNA and Protein Synthesis
RNA and Protein Synthesis

... Introduction: Inside a ribosome, amino acids are linked together to form a protein molecule. As the chain of amino acids grows, it folds and coils to form a three-dimensional shape. The complex shape that results determines the properties of the protein. Proteins have a wide variety of structures an ...
Protein Engineering
Protein Engineering

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Office Hours
Office Hours

... The study, which was published in the Sept. 3 issue of Cell, showed that stem cells taken from the hair follicles of mice could self-renew in a dish, and when grafted onto mice could grow into new follicles and hair. "We are now looking at whether we can isolate human cells with the same procedure," ...
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... -terminus with the elimination of a water molecule and the formation of the C-N peptide bond (Fig A.4 (b)). This reaction occurs in the ribosome and is the final step of the translation process. The geometry of the peptide group is planar and rigid. The Cα-C-N-Cα conformation is almost always trans, ...
Hybrid enzymes Pierre Béguin
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File

... Glucagon consists of only 1 alpha helix polypeptide. Glucagon breaks down glycogen into glucose when the body needs sugar for energy Integrin consist of two polypeptides with hydrophobic portion embedded in membrane. Used to connect between structures inside and outside the cell. The amino acid sequ ...
Membrane Bound: C2-Domain Abscisic Acid
Membrane Bound: C2-Domain Abscisic Acid

... cytosolic proteins can reside on the periphery of vesicles, and they can transiently interact with membranes for trafficking or signaling purposes; these associations are driven by protein modules that recognize specific features of proteins or membranes (Cho and Stahelin, 2005). The identities of t ...
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... Example of active transport: Na+/K+ pump (Na+ conc is higher outside cells). 3 Na+ ions bind to transporter protein inside cell. ATP phosphorylates protein, causes conformational change. The 3 Na+ ions are released outside cell; 2 K+ ions bound. Triggers dephosphorylation of protein. Protein goes ba ...
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... Composed of a core domain plus ATP and AMP lids ...
Chapter 3 Protein Synthesis
Chapter 3 Protein Synthesis

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Student Exploration Sheet: Growing Plants
Student Exploration Sheet: Growing Plants

... Introduction: Inside a ribosome, amino acids are linked together to form a protein molecule. As the chain of amino acids grows, it tends to coil and form a three-dimensional shape. The complex shape that results determines the properties of the protein. Proteins have a wide variety of structures and ...
Student Exploration Sheet: Growing Plants
Student Exploration Sheet: Growing Plants

... Introduction: Inside a ribosome, amino acids are linked together to form a protein molecule. As the chain of amino acids grows, it tends to coil and form a three-dimensional shape. The complex shape that results determines the properties of the protein. Proteins have a wide variety of structures and ...
Gizmos Protein Synthesis WS
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Topic 14: Protein Synthesis
Topic 14: Protein Synthesis

... 2. at the 3’ end in a site where a particular amino acid will be attached 3. consists of three loops; the middle of which corresponds to a site known as the anticodon site; it has base sequence that is complementary to codons on the mRNA 4. there are 41 different tRNA’s ; there are 61 different codo ...
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Proteomics studies of post-translational modifications in plants

... of proteins and a highly sensitive method for their detection. More than 300 different types of PTMs have been identified and new ones are regularly added to the list (Jensen, 2004). A single protein frequently presents a heterogeneous population of proteins with different PTMs at multiple sites tha ...
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... Hydropathy Plots for Alpha Helical Proteins: Classic Method For alpha-helical membrane proteins, you can use hydropathy plots to predict the probability that a segment will be within the membrane. These are generated by measuring, for each amino acid, its partition coefficient between water and a n ...
Chap 2-3 Notes - WordPress.com
Chap 2-3 Notes - WordPress.com

... Organic Chemistry : the study of all compounds that contain bonds between carbon atoms. Macromolecules: formed by a process known as polymerization. Monomers: small units that can join together with other small units to form  Polymers large compounds formed from combinations of many monomers Four g ...
The Essential Need for Protein Chemists
The Essential Need for Protein Chemists

... is that proteins are potentially capable of adopting different structural conformations, and this can profoundly influence critically-important properties such as function, solubility, bioavailability, half-life, aggregation, toxicity, and immunogenicity (3-5). In the simplest case, proteins can exi ...
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... Regulation is accomplished by sequence-specific DNA binding proteins. Binding may be promoter proximal or at a distance. DNA footprinting and mobility shift assays are used to investigate the binding of regulatory proteins. In the E. coli lac operon, there are both repressors and activators, each of ...
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TP+FP
TP+FP

... • Depending on gap penalties chosen, the algorithm might have difficulty with making such long gaps (for example when using high affine gap penalties), resulting in incorrect alignment. ...
notes 12B
notes 12B

... 2. DNA is a template for _______________ formation during _______________. 3. Transcription is the first step in gene _______________; it is the process whereby a DNA strand serves as a template for the formation of _______________. 4. During translation, an mRNA _______________ vdirects the sequenc ...
From the Cradle to the grave: molecular chaperones that may
From the Cradle to the grave: molecular chaperones that may

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Protein Synthesis - Overview
Protein Synthesis - Overview

... c3yU ...
Lost in translation - Botany - LMU Munich
Lost in translation - Botany - LMU Munich

... Despite the use of both in vitro and in vivo methods in Schwenkert’s research, it can be very difficult to study the stages of preprotein passage within the plant cell after translation in the cytosol. This is because the steps are very short-lived, and in vitro systems that have been used in the pa ...
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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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