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Amino Acid and Protein Structure
Amino Acid and Protein Structure

... Every protein in its native state has a unique three-dimensional structure, which is referred to as its conformation. The function of a protein arises from its conformation. Protein structures can be classified into four levels of organization: primary, secondary, tertiary, and quaternary. The prima ...
Ch 7 Slides - people.iup.edu
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... • In receptor-mediated endocytosis, binding of ligands to receptors triggers vesicle formation • A ligand is any molecule that binds specifically to a receptor site of another molecule • Some viruses enter in this way ...
Chlamydomonas reinhardtii strains carrying the stb1-1
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... spectrometry. For Pho A (a) the peptide displayed in bold faced red was identified as the Nterminus of the protein: The peptide is not preceded by a lysine or an arginine, (and, therefore, it can not originate from the tryptic digestion). Furthermore, the N-terminal alanine was shown to be acetylate ...
Here is the Original File - University of New Hampshire
Here is the Original File - University of New Hampshire

... Evidence from experimental characterization of structures of nucleic acids such as RNA suggests that nucleic acids are highly flexible similar to proteins, and can undergo large-scale conformational rearrangements due to motions encoded in their structure or due to binding of triggering factors such ...
The Chemical Building Blocks of Life
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... M. Tertiary structure of most proteins is flexible. N. Extreme conditions (temperature, pH, etc.) can denature proteins. 1. Some proteins lose biological function after denaturation. 2. Some organisms are adapted to function in extreme conditions. 3. Denaturation can be permanent or reversible. O. ...
Protein Purification Affinity purification
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Module IV Nucleus
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Protein Synthesis
Protein Synthesis

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and y-crystallin X - Prof. N. Srinivasan
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... locations of these proteins in the lens. y-Crystallins are found mainly in the central densely packed core region of the lens, whereas yS-crystallin occurs in the more hydrated outerregion: this has led to the notion that their different interactions with protein and solvent may contribute to the ov ...
Signal Transduction
Signal Transduction

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The proteome of Saccharomyces cerevisiae mitochondria
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... known subunits of the pyruvate dehydrogenase complex, the tricarboxylic acid cycle, and the inner membrane complexes of the oxidative phosphorylation machinery, including the eight stable proteins that are encoded by the mitochondrial genome. Because most of the latter proteins are hydrophobic prote ...
RNA
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... There are four main differences between RNA and DNA: • The sugar in RNA is ribose instead of deoxyribose. • RNA is single-stranded. DNA is double-stranded. • RNA contains uracil in place of thymine. • DNA stays in the nucleus, but RNA can leave the nucleus and go into the cytoplasm. ...
Bacterial Systems for Assembly, Secretion and Targeted
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... Type III system A battery of toxins of human enteropathogens, such as Yersiniae, Salmonellae and enteropathogenic Escherichia coli, use this system to carry out the invasion of host intestinal epithelial cells (Fig. 1F). A Type III system is also used by Pseudomonas syringae and other plant pathogen ...
RNA Synthesis
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... • Gly-­‐Asp-­‐Asp  in  all  (+)  strand  RNA  polymerases • Asp-­‐Asp  in  RT,  segmented  (-­‐)  strand  polymerases • Gly-­‐Asp-­‐Asn  in  nonsegmented  (-­‐)  strand  polymerases;  birnaviruses   have  Ala-­‐Asp-­‐Asn ...
Genetic regulation of eukaryotes
Genetic regulation of eukaryotes

... II.1.5. Alternative gene usage (24. – 26. slides) Alternative promoter usage means that a gene can be transcribed from various promoters in different tissues, resulting in proteins with varying length or with varying amino acid sequences if alternative splicing also occurs. Alternative polyadenylati ...
doc - Gogarten Lab
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... e. The hypothesis that the entire Earth is the unit of life and the entire biosphere is alive, because almost no single species can exist in complete isolation from other forms of life. It also includes the notion that the ecosystems on the Earth are protected by negative feedback loops that help ma ...
bch2ibm: molecular biology end of semester 1 exam notes 2014
bch2ibm: molecular biology end of semester 1 exam notes 2014

... -­‐ It’s  a  ribosomal  binding  site  in  mRNA,  generally  located  8  basepairs   upstream  of  AUG   -­‐ Exists  only  in  prokaryotes   -­‐ The  six-­‐base  consensus  sequence  is  AGGAGGU  –>  this  sequence  helps   recruit  the  ri ...
PHD domains and E3 ubiquitin ligases: viruses make the connection
PHD domains and E3 ubiquitin ligases: viruses make the connection

... requires the PHD motif. These are the first examples linking the PHD domain to E3 activity, but the recent discovery of PHD-dependent E3 activity in the cellular kinase MEKK1 and the close structural relation of PHD domains to RING fingers hint that many other PHD proteins might share this activity. ...
How do we purify proteins? GFP as model system to learn
How do we purify proteins? GFP as model system to learn

... GFP Structure ...
Thermodynamic prediction of protein neutrality
Thermodynamic prediction of protein neutrality

... the first few substitutions (33). Proteins that sit on the very margin of the minimal stability threshold exhibit lower 1-neutrality than is predicted by an exponential decline because these proteins are less stable than the average folded protein; thus, surviving sequences will tend to be more stab ...
1 Abstract
1 Abstract

... on hydration. A 2D (Tricine-Tris) SDS-PAGE protein separation system was also used in attempts to isolate novel low molecular weight proteins from the pollen coats of both B. oleracea and A. thaliana. Here, results indicate that at least two of the four isoforms of the PCP-B family (PCP-Bβ and PCP-B ...
gene transcription and rna modification
gene transcription and rna modification

... Also as heterogeneous nuclear RNA (hnRNA) ...
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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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