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Protein Synthesis - SCF Faculty Site Homepage
Protein Synthesis - SCF Faculty Site Homepage

... • The location for protein synthesis – the workbench on which a polypeptide is built. • rRNA makes up a RIBOSOME. • Ribosomes have 2 sub-units. ...
Prok transcription
Prok transcription

... there are 2 types of sequence signalling termination 1. rho independent termination/intrinsic termination there is formation of a stable GC rich stem-loop in the newly synthesized RNA followed by a string of U's (A's in the template strand) spaced about 20 bases downstream (these sites are often cal ...
Chapter-1-Structure-and-Variety-of-Protein
Chapter-1-Structure-and-Variety-of-Protein

... sequence of Amino Acids • Weak chemical links called HYDROGEN BONDS form between certain amino acids in a polypeptide chain. • This causes the chain to become coiled and spiral (HELIX). This is the Seconday structure! ...
Lecture2
Lecture2

... Regulation of Protein Function Regulation of protein function allows the cell to regulate not only the amounts but also the activities of its proteins. There are three general mechanisms of control of cellular proteins: • regulation by small molecules - most enzymes are controlled by changes in conf ...
Presentation Slides II - Vandiver, June 29, 2016
Presentation Slides II - Vandiver, June 29, 2016

... The Star BioChem computer activity requires a working knowledge of these four levels. Summary slide of key concepts for proteins is next….. ...
Genetic Code and Transcription
Genetic Code and Transcription

... – RNA PolIII ...
Protein And Amino Acids - Manasquan Public Schools
Protein And Amino Acids - Manasquan Public Schools

... contains all the essential amino acids in relatively the same amounts that human beings require.  Complementary proteins- two or more incomplete proteins whose amino acid assortments complement each other in such a way that the essential amino acids missing from one are supplied by the other. ...
1 Glycosylation and Protein Folding I. Introduction. As a translocated
1 Glycosylation and Protein Folding I. Introduction. As a translocated

... I. Introduction. As a translocated polypeptide emerges into the lumen of the ER, it is generally processed in three ways: 1) its signal sequence is cleaved by signal peptidase; 2) it is glycosylated; and 3) it must be helped to fold into the correct conformation. II. Signal peptidase. Cleavage of th ...
Acids
Acids

... The actual #s are ridiculous. 0.0000001, 0.000001, etc. If take –log of 0.0000001 it becomes 6, 7, etc pH is the negative log of the H+ concentration Scale is 0-14 Smaller # means more free H+ Each whole number means 10X difference in [H+] ...
Full size lecture slides (PDF file, 660 kB)
Full size lecture slides (PDF file, 660 kB)

... polypeptide chain – this folding is determined by where the hydrophobic and hydrophilic amino acids are • Once secondary structure has formed it folds back upon itself to form an even more stable molecule: tertiary structure. • If a protein consists of more than one amino acid chain, the arrangement ...
Organic Molecule Cut-Outs
Organic Molecule Cut-Outs

... rectangle, and the words “Proteins,” “polymer,” and “monomers.” 2. Arrange the cut-outs so that the Amino Acids form a protein (don't worry about the order of the amino acids). Include the equal sign; you will have an amino acid chain equaling a protein. 3. Glue down your cut-outs. 4. Glue the “mono ...
From Gene to Protein - Jackson School District
From Gene to Protein - Jackson School District

... tRNA= carries a specific amino acid to ribosome based on its anticodon to mRNA codon rRNA= makes up 60% of the ribosome; site of protein synthesis snRNA=small nuclear RNA; part of a spliceosome. Has structural and catalytic roles srpRNA=a signal recognition particle that binds to signal ...
Design and chance in the self
Design and chance in the self

... glycolytic enzyme enolase, whose function is still yet to be determined. In vivo studies indicate that enolase may have a role in regulating gene expression in conjunction with small regulatory RNAs [32]. Molecular genetic studies show that the degradosome contributes to global regulation of mRNA le ...
duplicativenetworks
duplicativenetworks

... Proteins are produced and degraded all of the time. The rates at which these processes occur depend on what proteins are already present, how they interact with one another directly and how they interact with genes (at DNA or mRNA level). Proteins that bind to DNA or RNA have direct effect on produc ...
LC/MS Study of Casein Proteins in Milk
LC/MS Study of Casein Proteins in Milk

... Cows, depending on the breed, have genetic variants resulting in the production of different sequences of beta-casein. Older breeds of African and Indian cows and water buffalo have the A2 beta-casein genetic allele and produce only this protein. Some cows, such as Holsteins and Friesians, have a ge ...
PROTEINS – STRUCTURE AND FUNCTION (DR. TRAISH)
PROTEINS – STRUCTURE AND FUNCTION (DR. TRAISH)

... 2. hydrogen bonding, hydrophobic interactions, electrostatic interactions, van der Waals’ forces all stabilize conformation 3. For many proteins, tertiary is the highest level of structure iv. Quaternary Structure 1. When there is more than one subunit (even if they are all the same) 2. Structure fo ...
Protein Synthesis
Protein Synthesis

... The Genetic Code  All organisms use the same genetic code.  UUU codes for phenylalanine in redwood trees, bacteria, and you and me. ...
BS3 Crosslinking
BS3 Crosslinking

... agent, which selectively crosslinks cell-surface proteins to form high-molecular-mass aggregates. Because intracellular proteins are not modified, they retain normal molecular mass. This enables surface and intracellular pools of a particular protein to be distinguished by SDS–PAGE and Western blott ...
Transcription and RNA processing
Transcription and RNA processing

... In bacterial cells, the holoenzyme (RNA polymerase plus sigma) recognizes and binds directly to sequences in the promoter. In eukaryotic cells, promoter recognition is carried out by accessory proteins (transcription factors) that bind to the promoter and then recruit a specific RNA polymerase (I, II ...
Protein Digestion and Absorption
Protein Digestion and Absorption

... Proteins are sequences of amino acids (AA) linked by peptide bonds. There are twenty amino acids of which nine are essential and eleven are non-essential. Essential amino acids include phenylalanine, valine, threonine, tryptophan, isoleucine, methionine, leucine, lysine, and histidine. These AA are ...
DNA vs. RNA - WordPress.com
DNA vs. RNA - WordPress.com

...  Similar signals in DNA cause transcription to stop when the new RNA molecule is completed. ...
No Slide Title
No Slide Title

... 1) Engineers make the design and tell the workers how to make the cars; 2) Workers follow the directions to build the cars; 3) Suppliers bring parts to the assembly line so they can be installed in the car ...
DNA Functions
DNA Functions

... -  The DNA of eukaryotic genes contains sequences of nucleotides, called introns, that are not involved in coding for proteins. -  The DNA sequences that code for proteins are called exons. -  When RNA molecules are formed, introns and exons are copied from DNA. ...
Nucleic acids and their protein partners
Nucleic acids and their protein partners

... without the help of proteins. Electrostatics is a dominant force in RNA folding, but recent theoretical, computational, and experimental investigations have revealed the interplay of counterions, RNA structure and folding pathways. New structural methods, including timeresolved footprinting, small-a ...
Transcription and Translation
Transcription and Translation

... No effect if it is the same amino acid  Redundancy! Missense – codes for a different amino acid Nonsense – codes for a stop codon Can be harmful to the organism if a useless or less active protein is created. ...
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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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