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Sample Questions 1 - U of L Class Index
Sample Questions 1 - U of L Class Index

... structure. The single “A” subunit has a molecular mass near 22 kDa and each “B” subunit has a mass of near 12 kDa. (a) Sketch and label a figure of the result of an SDS-PAGE experiment. (b) Sketch and label a figure of the result of size exclusion chromatography experiment. (26) What is the retardin ...
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BioH From DNA to proteins
BioH From DNA to proteins

... The initiator tRNA anticodon-mRNA codon bond causes the next bonding site in the ribosome to attract the specific anticodon of another tRNA A 2nd tRNA (with its amino acid) bonds with the 2nd m RNA codon Once this happens, enzymes help form a peptide bond between the two nearby amino acids While oth ...
Questions with Answers
Questions with Answers

... Cytosol: mRNA simply gets transcribed by free ribosome. All proteins that do not have a sorting signal remain in the cytosol by default. ER lumen (pre-modifications that occur in golgi): polypeptide has signal sequence near amino teminus which that causes SRP to bind, which stops translation and the ...
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AP Biology Discussion Notes

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Dietary Protein Quality: Its importance in Nutrition and Health
Dietary Protein Quality: Its importance in Nutrition and Health

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Introduction to Carbohydrates
Introduction to Carbohydrates

... synthesized by transfer of an amino group to the α-keto acids pyruvate, oxaloacetate, and αketoglutarate, respectively. • These transamination reactions (Figure 20.12, and see p. 250) are the most direct of the biosynthetic pathways. • Glutamate is unusual in that it can also be synthesized by the r ...
Ch03Pt1.doc
Ch03Pt1.doc

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AMINO ACIDS, POLYPEPTIDES, AND PROTEINS

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transcription_ translation and protein synthesis REGULAR

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From boron analogues of amino acids to boronated DNA

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Liver Function - Wk 1-2

... form a different N-containing compound. Newly ingested amino acids, as well as derivatives from the Krebs Cycle are taken up by the cells of the liver via active transport processes and used to replace and/or synthesise new proteins. These include albumin, prothrombin, acute phase proteins, clotting ...
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Organic Chemistry - Biology Junction

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Organic Chemistry - Welcome to Cherokee High School

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Problem Set 3 (Due February 4th) 1. In 1896, Christiaan Eijkman
Problem Set 3 (Due February 4th) 1. In 1896, Christiaan Eijkman

... mechanism relates to the ‘dietary’ carbon source. E. coli Isocitrate Dehydrogenase (IDH) can be inhibited by the activity of another enzyme, IDH kinase/phosphorylase (gene aceK). This enzyme, which is part of an operon containing genes for Malate Synthase and Isocitrate Lyase (the two enzymes of the ...
Lecture Slides for Nitrogen Metabolism
Lecture Slides for Nitrogen Metabolism

... The universal product of degrading amino acids is ammonia. • Ammonia is toxic at not very high concentrations. • You have to get rid of it. • If you are an aquatic organism, you can just diffuse in into the environment. • We convert ammonia to urea. The basic idea: • Add the nitrogens to ornithine t ...
BY 330 Summer 2015Mock Exam 2 Ten molecules of
BY 330 Summer 2015Mock Exam 2 Ten molecules of

... for this conversion, including all intermediates and energy production sites. (I won’t show the pathway for the conversion, but it is the process of glycolysis starting at G3P and ending at pyruvate. This will come straight from your notes. Make sure you show all of the carbon intermediates, where A ...
< 1 ... 495 496 497 498 499 500 501 502 503 ... 622 >

Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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