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Gelatinization of Starch
Gelatinization of Starch

... Aliphatic Side Chains ...
Proteins and amino acids
Proteins and amino acids

...  The sticky amino acids glue together  The non-sticky amino acids point to the water  The waters must be ‘happy’ ...
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... and lam), and possibly higher legumin content in the case of lam, had lower total protein contents. The relative proportions of the 2S±4S (albumin) fraction in wild-type and mutant lines were also highly different. Those mutants with reduced levels of legumin appeared to be associated with compensat ...
CHAPTER 6 Gene Expression: Translation
CHAPTER 6 Gene Expression: Translation

... d. It is almost universal. In nearly all organisms studied, most codons have the same amino acid meaning. Examples of minor code differences include the protozoan Tetrahymena and mitochondria of some organisms. e. It is degenerate. Of 20 amino acids, 18 are encoded by more than one codon. Met (AUG) ...
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... d. uracil 57. bonds that are found in a secondary protein structure a. hydrogen 58. bonds found in triacylglycerol a. ester ...
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... binding proteins that enhance import of purified precursors have been described(l4,l’).So far, the role of such proteins in the intact cell remains to be demonstrated. Several lines of evidence, on the other hand, have strongly suggested an important function for cytosolic heat shock proteins (ct-hs ...
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Adaptation of proteases and carbohydrases of

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SBI 4UI Review of Biochemistry Name: Learning Goals R Y G

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The Effect of Protein Loads on Plasma Amino Acid Levels
The Effect of Protein Loads on Plasma Amino Acid Levels

... (Felig, 1973). The branched-chain amino acids are deaminated more slowly than other amino acids in the liver, and normally depend on the extrahepatic tissues for their metabolism (Miller, 1962; Ning, Lowenstein & Davidson, 1967; Felig, 1973). This explains the finding that they show the most sustain ...
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... molecules to their basic components. Several organs produce enzymes that break down specific food molecules. The mouth contains amylase, an enzyme from saliva that breaks starches (polysaccharides) into disaccharides. Cells in the lining of the stomach produce pepsin, which in the presence of hydroc ...
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... Most metabolic reactions depend on chemical energy. a. This form of energy is held within the chemical bonds that link atoms into molecules. b. When the bond breaks, chemical energy is released. c. This release of chemical energy is termed oxidation. d. The released chemical energy can then be used ...
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... (including those made from carbohydrates) are stored away in cells of adipose tissue. 2. Because fatty acids have many more carbon and hydrogen atoms, they yield greater amounts of ATP. C. Energy from Proteins Amino group is released as ammonia in urine. The amino acid remnant is fed into the Krebs ...
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... • Proteins are polymers of amino acid monomers. – Twenty different amino acids are used to build proteins in organisms. – Amino acids differ in side groups, or R groups. – Amino acids are linked by peptide bonds. ...
CPP1
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... protein of POR 1 (CPP1), an essential protein for chloroplast development, plays a role in the regulation of POR stability and function. CPP1 contains a J-like domain and three transmembrane domains and is localized in the thylakoid and envelope membranes, and interacts with POR isoforms in chloropl ...
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... • Explain that the adrenaline receptor is located in the cell’s plasma  membrane, where it can encounter adrenaline that has been released into  the bloodstream as a signal of danger.  • Show the membrane view, and explain that only a small “plug” or section  of the cell membrane surrounding the str ...
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... residues produced STD effects at the aromatic protons. Substitution at Ser4 position for Asn produced STD effects that were similar in pattern and intensity to those of the native sequence. The results indicate that the Pro6 residue is critical for antibody binding and substitution at this position ...
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... 2005; Liceaga-Gesualdo & Li-Chan 1999). The functional properties of fish protein hydrolysates prepared may be improved through partial hydrolysis where the proteins are hydrolyzed to the desired extent by the use of specific enzymes and by choosing a defined set of hydrolysis conditions. Parameters ...
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29. protein targeting and degradation

... signal-binding protein α-karyopherin (or α-importin) with a nuclear localization signal peptide bound to its major recognition site. ...
2.3 Carbon-Based Molecules
2.3 Carbon-Based Molecules

... – Twenty different amino acids are used to build proteins in organisms. – Amino acids differ in side groups, or R groups. – Amino acids are linked by peptide bonds. ...
P-glycoprotein Activation Monitored via ATP Hydrolysis and ATP
P-glycoprotein Activation Monitored via ATP Hydrolysis and ATP

... evaluated with a model taking into account activation with one, and inhibition with two molecules bound to P-glycoprotein (1, 2). The experiments revealed that the concentrations of half-maximum P-glycoprotein activation, K1, were identical in insideout plasma membrane vesicles and in living cells a ...
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Metabolic fate of amino acid

... • Intracellular proteases hydrolyze internal peptide bonds, of protein releasing peptides, which are then degraded to free amino acids by peptidases. • Endopeptidases cleave internal bonds, forming shorter peptides. • Amino peptidases and carboxy peptidases remove amino acids sequentially from the ...
2 Applications
2 Applications

... regulation e.g. preventing digestive proteases from attacking gastric cells.  Digestion of dietary proteins: Dietary proteins are gradually degraded to individual amino acids in order to be of use to the organism. This process is catalyzed by digestive proteases. When food reaches the stomach, peps ...
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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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