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Biomolecules
Biomolecules

... Monomers that make up proteins Each has same fundamental structure: 1. Central Carbon back 2. Amino group (NH2) bone 3. Carboxyl group (COOH) 4. R group - variable ...
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... EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen. EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, ...
Biological Molecules - Princeton High School
Biological Molecules - Princeton High School

... Shape can be influenced by factors like temperature and solvent) … for example, egg white is clear when it is uncooked, and white when it is ...
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5 Kingdoms of Life - Cellular

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Ch18_PT MULTIPLE CHOICE. Choose the one alternative that best

... bonds with water because of their polarity E) the form of an amino acid in which both the carboxyl group and the amine group are charged, but the overall molecule remains neutral F) a carbon atom bonded to four different groups and therefore able to form enantiomers G) a protein with the tertiary st ...
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Close Reading for Macromolecules
Close Reading for Macromolecules

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Chapter 2 Review Sheet Name:_______________________
Chapter 2 Review Sheet Name:_______________________

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Intermediary Metabolism-II SECTION A What are ketogenic amino

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Enzymeregulation
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B2 Topic 1 The Components of Life

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AMINO ACIDS I. Function of amino acids A. Building blocks of

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Lecture 19

... that form the backbone of a peptide chain or protein The secondary structures of proteins indicate the three-dimensional spatial arrangements of the polypeptide chains The tertiary structure of a protein gives a specific three-dimensional shape to the polypeptide chain including interactions and cro ...
Chapter 19 Aminoacids and Proteins
Chapter 19 Aminoacids and Proteins

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A. biotin

... An attempt is made to separate proteins A, B, and C of molecular weights 100,000 (C), 50000 (B) and 25000 (A) Daltons respectively, by chromatography using G-50 Sephadex. The order of elution of these proteins sequentially from this column is expected to be A. B. C. D. ...
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26.4 The ureo cyde

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Protein primary structure: Amino acids
Protein primary structure: Amino acids

... stability of proteins. Despite the simplicity of its molecular structure, water shows very unusual properties. For example, water expands upon freezing transition and, in fact, expands even in the liquid form when temperature is reduced from 4°C to 0°C. Water also has an unusually large heat capacit ...
Dehydration Synthesis 2.cwk
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... Dehydration Synthesis Activity For each section, you will be simulation the dehydration synthesis reaction. In other words, you will be removing water in order to join together two (or more) molecules. Use your book and notes to get an idea of the building block molecules you are using (sugars, glyc ...
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QUIZ #7 NUCLEOTIDE METABOLISM
QUIZ #7 NUCLEOTIDE METABOLISM

... b. Cytidine c. Cytosine d. Guanosine e. Uridine ...
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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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