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Notes - Part 2.
Notes - Part 2.

... The actin-dependent ATP-hydrolyase (ATPase) activity is localised in the globular heads of myosin (labelled S1) each of which also binds two different "light chains". The enzyme-catalysed reaction involves a profound conformational change in the structure of S1. It was one of the first enzymes for w ...
BCM 6200 - Purification des proteines membranaires
BCM 6200 - Purification des proteines membranaires

... Crystallization Methods (Lipidic-cubic phase - LCP): Lipidic cubic phase (LCP) is one of many liquid crystalline phases that form spontaneously upon mixing lipids with water at proper conditions. The protein is mixed with Monoolein and other lipid additives in tightly coupled syringes. Drops are la ...
Lecture 8
Lecture 8

... gradiennt in the presence of high voltage. • Can also use gels with immobilized pH gradients -made of acrylamide derivatives that are covalently linked to ampholytes. Used with a gradient maker to ensure continuously varied mixture when the gel is made. ...
- Academy Test Bank
- Academy Test Bank

... 87) Which of the following statements about the genetic code is TRUE? A) A single gene contains only those nucleotides that code for a single protein. B) A single codon may code for more than one amino acid. C) Termination codons do not code for amino acids. D) The promoter sequence is found on the ...
ppt
ppt

... • Proteins from ER are processed and sorted for transport: to endosomes, lysosomes, plasma membrane, or secretion. • Most glycolipids and sphingomyelin are made in Golgi, • The Golgi is composed of flattened membrane-enclosed sacs (cisternae) and associated vesicles: ...
CH 17 PPT
CH 17 PPT

... Aminoacyl-tRNA synthetase—a type of enzyme that catalyzed the attachment of amino acid to its tRNA. Each of the 20 amino acids has a specific aminoacyltRNA synthetase. 2 steps in attachment of an amino acid: Activation of the amino acid with AMP. The synthetase’s active site binds the amino acid and ...
Chapter 22 (Part 2)
Chapter 22 (Part 2)

... • In E. coli RF-1 recognizes UAA and UAG, RF-2 recognizes UAA and UGA. • RF-3 binds GTP and enhances activities of RF-1 and –2. • Presence of release factors with a nonsense codon at A site transforms the peptidyl transferase into a hydrolase, which cleaves the peptidyl chain from the tRNA carrier • ...
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Polypeptide Synthesis - Fairfax Senior High School
Polypeptide Synthesis - Fairfax Senior High School

... Forming a polypeptide  Once 1st two aa are in place, 1st tRNA is then released  Leaving it free to pick up another aa  Process continues-ribosomes moves along mRNA  Polypeptide chain grows  Aa added to a chain at 15/s  One of 3 codons stop the translation process  No tRNA to match up  Trans ...
Preview Sample 1
Preview Sample 1

... A) the bond between two molecules is broken, resulting in the removal of a water molecule. B) the bond between two molecules is broken through the splitting of a water molecule, thereby creating two new bonds with the H and OH of that water in its place. C) two molecules are joined together, resulti ...
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RNA polymerase II
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news and views Mechanics of the ribosome
news and views Mechanics of the ribosome

... formed (see Box 1). One of these regions is a small stretch of 23S rRNA; the other is a protein–RNA complex. Both of these regions have previously been isolated from the ribosome and analysed by NMR spectroscopy and X-ray diffraction6,13. Conformational transitions in these regions can be inhibited ...
Signal Transduction Pathways • Signal Transduction
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... and activation of the insulin receptor •How is the activation loop phosphorylated? –the two α subunits move together to surround one insulin molecule, the kinase domains also draw closer together –the two β subunits forced together, the kinase domain catalyze the phosphoryl groups from ATP to tyrosi ...
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... Non-coding RNAs or RNAs come more than in three flavours... ...
AP Biology
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... – Proteins are polymers of amino acids joined by peptide bonds – All amino acids have a similar structure – All contain amino and carboxyl groups – All have a variable “R” group ...
ppt link
ppt link

... Missense mutations: replace one amino acid codon with another Nonsense mutations: replace amino acid codon with stop codon Splice site mutations: create or remove exon-intron boundaries Frameshift mutations: alter the ORF due to base substitutions Dynamic mutations: changes in the length of tandem r ...
Biol 1020 Ch. 5: types of organic molecules
Biol 1020 Ch. 5: types of organic molecules

... pay attention to what makes an R group polar, nonpolar, or ionic (charged) and thus their hydrophobic or hydrophilic nature ...
S1936878X10003839_mmc1 - JACC: Cardiovascular Imaging
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... Superscript II reverse transcriptase (Invitrogen, Carlsbad, California) and oligo-dT primers (Invitrogen) as follows. One microgram of total RNA from each sample was used for cDNA synthesis. RNA and oligo-dT primers were incubated for 3 min at 70°C to allow primer annealing, after which the tubes we ...
Assignment 5 (Perl Project 2)
Assignment 5 (Perl Project 2)

... and t in any order. For example, acgtacccggttt is a small DNA strand. The four letters stand for the four nucleotides : adenine, cytosine, guanine, and thymine. Nucleotides, which are the molecular units from which DNA and RNA are composed, are also called bases. A special enzyme called RNA polymera ...
Synthesis of biopolymers: proteins, polyesters
Synthesis of biopolymers: proteins, polyesters

... direct the synthesis of proteins and thus determine the characteristics of organisms.In addition to the very specific relations between structure and function, another aspect of biopolymers intriguing to materials scientists is the precision with which they are made. In contrast to conventional synt ...
Ribosome locations
Ribosome locations

... Eukaryotes have 80S ribosomes, each consisting of a small (40S) and large (60S) subunit. Their 40S subunit has an 18S RNA (1900 nucleotides) and 33 proteins.[15][16] The large subunit is composed of a 5S RNA (120 nucleotides), 28S RNA (4700 nucleotides), a 5.8S RNA (160 nucleotides) subunits and 46 ...
Differentially Expressed Proteins in Sugarcane Leaves
Differentially Expressed Proteins in Sugarcane Leaves

... and relative water content (RWC) were recorded to quantify the water deficit stress. Leaf proteins from non- and water-stressed plants were separated using two-dimensional electrophoresis (2-DE). Image analysis was performed on the electrophoresis gel to locate proteins that were differentially expr ...
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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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