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... Receptor tyrosine kinase is a transmembrane protein which is normally inactive. When the ligand binds (e.g. insulin), the receptor subunits aggregate, and the tyrosine molecules become phosphorylated other intracellular proteins then bind to the tyrosine kinase and are activated ...
Molecules - Chapter 2
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... 1. Has 4 Valence electrons 2. Forms 4 covalent bonds (single, double, or triple) with oxygen, nitrogen, phosphorous, and sulfur 3. Can form chains - straight, branching or rings - varies in length, number and location of double bonds and presence of other elements 4. Forms ISOMERS (same chemical for ...
Cytoskeleton Handout
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... repeats. Heptad repeats promote the association of parallel α-helices into a structure known as a coiled-coil. Intermediate filament proteins assemble into dimers via coiled-coil interactions. The basic unit of intermediate filaments are possibly tetramers formed from dimers in a head-to-tail orient ...
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... 4. There is at least one _______________ molecule for each of the 20 amino acids found in proteins. 5. There are fewer _______________ than codons because some tRNAs pair with more than one codon; if an anticodon contains a U in the third position, it will pair with either an A or G–this is called t ...
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... 3. protein - peptide with 100 or more amino acids major functions: a. structure b. contraction c. transport d. buffers e. enzymes f. hormones g. antibodies function depends on 3-dimensional structure structure depends on bonds between amino acids if the bonds are broken, the shape changes and the pr ...
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Macromolecules
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... EWPP confirmed the different cleavage patterns of the investigated proteolytic enzymes. All the products of the enzymatic treatment of EWPP were eluted from 10 to 53% of acetonitrile. However, the distribution of peaks were significantly different. The  antioxidative capacities of  the  EWPP hydroly ...
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Download PDF
Download PDF

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basic principles of isoelectric focusing in biomedical engineering

... point, it has no net charge and cannot be moved in a gel matrix by the electric field. It may, however, move from that position by diffusion. The pH gradient forces a protein to remain in its isoelectric point position, thus concentrating it; this concentrating effect is called "focusing". Increasin ...
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... 2. A researcher was studying the kinetic properties of β-galactosidase using an assay in which οnitrophenol-β-galactoside (ONPG), a colorless substrate, is converted to galactose and onitrophenolate, a brightly-colored, yellow compound. Upon addition of 0.25 mM substrate to a fixed amount of enzyme, ...
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Proteolysis



Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Low pH or high temperatures can also cause proteolysis non-enzymatically.Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells. Consequently, dis-regulation of proteolysis can cause diseases, and is used in some venoms to damage their prey.Proteolysis is important as an analytical tool for studying proteins in the laboratory, as well as industrially, for example in food processing and stain removal.
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