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Ribosomes: Cashing in on crystals
Ribosomes: Cashing in on crystals

... density map and a complete atomic model may be available in the near future. A similar level of atomic detail is seen in the 5.5 Å resolution map of the 30S ribosomal subunit from the bacterium Thermus thermophilus. Clemons et al. [3] produced a map of the small subunit with the characteristic shape ...
Chapter 1
Chapter 1

... A priori, one would expect that sugars bind with a higher affinity to the outside facing binding site than to the inside facing binding site, that is the site from where the sugar, which is taken up, has to be released. However, this is not necessarily true for a system like LacS, where following re ...
Functional Control by Codon Bias in Magnetic Bacteria
Functional Control by Codon Bias in Magnetic Bacteria

... bias residing in the Magnetospirillum magnetotacticum genome. While primary sequences of flagellar, iron uptake and the house-keeping RNA polymerase proteins are identical in magnetic bacteria compared to E. coli and mammalian cells, there is no genetic similarity for flagellar and iron uptake protein ...
DNA Lesson Plan - Penn Arts and Sciences
DNA Lesson Plan - Penn Arts and Sciences

... show the 5’ and 3’ ends of the helix, stress this orientation for RNA transcription. Figure 6 ends the review of DNA structure as it positions all of the structures into the helix. Students should see the location of the bases and be reminded that their sequence codes genetic information. Table 1 sh ...
Visualization of RNA molecules using VMD
Visualization of RNA molecules using VMD

... thymine as a base pair to adenine. It is also single-stranded in most cases, while DNA is double-stranded. The sugar is ribose in RNA and deoxyribose in DNA. ...
Chapter 14 Proteins
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- Wiley Online Library
- Wiley Online Library

... Current evidence indicates that RNA molecules undergo diverse metabolic processes as a result of developmental or environmental cues, although the molecular mechanisms are largely unknown (for review see Dreyfuss et al., 1988). An increasing number of developmentally important RNPs have been identif ...
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please click, ppt - Department of Statistics | Rajshahi University
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... molecular weight (HMW) complex functioning as a chaperone. The N-terminal peroxidatic Cys residue acting as a sensor of H2O2 concentration in the cell and the C-terminal tail of eukaryotic 2-Cys Prxs containing a ‘YF-motif’ play critical roles in this structural and functional transition [6–8]. Also ...
elisa - WordPress.com
elisa - WordPress.com

... applications including ELISA and immunohistochemistry. • It is also used as a nutrient in cell and microbial culture. • In restriction digests, – BSA is used to stabilize some enzymes during digestion of DNA – prevent adhesion of the enzyme to reaction tubes and other vessels. ...
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... applied. The proteins will migrate to their isoelectric pH, the location at which they have no net charge. (B) The proteins form bands that can be excised and used for further experimentation. Two-Dimensional Gel Electrophoresis. (A) A protein sample is initially fractionated in one dimension by iso ...
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... gene products by large-scale genomic and proteomic initiatives has required the development of high-throughput strategies to elucidate their function [8]. There have primarily been two approaches to characterize multiple proteins in biological samples. The first approach, 2D-gels, has been widely us ...
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... a- and /3-Tropomyosin (16, 17) consistently comigrated with the bands H10 and H5, respectively. Preliminary studies (see below) suggest that these are H n R N P proteins rather than a- and fltropomyosin. Bands C10, D1, and D4, which occur in both the washes and are prominent on washed nuclei, have b ...
Self-association of the SET domains of human ALL-1 and of
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... (Lewis, 1978). The pattern is initially established by the gap and pair-rule genes and is later maintained by the trithorax and polycomb group genes, which function as transcriptional activators and repressors, respectively. ALL-1 contains several motifs shared with other proteins. These include: (a ...
The role of protein–protein interactions in the intracellular traffic of
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... interact with TASK-1 [88]. Screening of a human heart cDNA library with the last 16 amino acids of human TASK-1 independently yielded 14-3-3β as an interacting protein [76]. Progressive truncation of the C-terminus from the proximal side showed that the last 40 amino acids of TASK-1 contributed to t ...
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RNA and Protein Synthesis

... 4. This single strand of RNA is now known as messenger RNA or mRNA and it now has a copy of DNA’s code for making proteins. ...
Applications of recombinant DNA technology in
Applications of recombinant DNA technology in

... gene. The core promoter is situated with a TATA and initiator (Inr) sequences. The TATA sequence, located 30 base pairs upstream of the Inr sequence, is the binding site for the TATA-binding protein. The Inr sequence is where RNA polymerase II binds and initiates transcription. The promoter proximal ...
ESCHERICHIA COLI
ESCHERICHIA COLI

... due to their ability to adapt against antimicrobial agents by the help of spontaneous mutation or by DNA transfer and differential protein expression. This process facilitates the resistance towards the action of certain antibiotics, making the antibiotic action ineffective [1]. During severe infect ...
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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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