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presentation source
presentation source

... • Examination of the genome alone can not take into account complex multigenic processes such as ageing, stress, disease or the fact that the cellular phenotype is influenced by the networks created by interaction between pathways that are regulated in a coordinated way or that overlap ...
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... Chaperonins. Large, double-ring structures that accept non-native proteins inside their cavities and assist protein folding. The eukaryotic cytosolic chaperonin is involved in folding actins and tubulins. Prefoldin. Hexameric molecular chaperone also involved in actin and tubulin biogenesis. Its exi ...
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... Fibrous proteins are formed from long polypeptide chains that are arranged parallel or nearly parallel to one another. Fibrous polypeptide chains form long strands or sheets and because of many hydrophobic amino acid residues, they are water insoluble but strong and flexible. These long fibers or sh ...
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... next section, along with the post-lab assignment. 1. (10 points) Polyacrylamide gel electrophoresis separates molecules based on their molar mass. a) (5 points) We measure protein mass in units of “Daltons” (“Da”), named after John Dalton who helped establish our understanding of the atomic nature o ...
Protein
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Protein phosphorylation



Protein phosphorylation is a post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or modifying its function. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. The amino acids most commonly phosphorylated are serine, threonine, and tyrosine in eukaryotes, and histidine in prokaryotes, which play important and well-characterized roles in signaling pathways and metabolism. However, many other amino acids can also be phosphorylated, including arginine, lysine, and cysteine. Protein phosphorylation was first reported in 1906 by Phoebus Levene at the Rockefeller Institute for Medical Research with the discovery of phosphorylated vitellin. However, it was nearly 50 years until the enzymatic phosphorylation of proteins by protein kinases was discovered.
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