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4 – 2 Chemical Compounds in Living Things
4 – 2 Chemical Compounds in Living Things

... o Ex: starch, cellulose (plants), glycogen (animals)  Complex carbohydrates (di- & polysaccharides) are produced by polymerization where 2 or more monosaccharides (monomers) combine to form larger molecules (polymers) o This process is called DEHYDRATION SYNTHESIS (dehydration=loss of water, synthe ...
Stabilization of Low Affinity Protein-Protein Interactions by
Stabilization of Low Affinity Protein-Protein Interactions by

Paper - IndiaStudyChannel.com
Paper - IndiaStudyChannel.com

... 12. Fructosuria is the result of : (A) a deficiency of phosphofructokinase (B) a deficiency of liver fructokinase (C) elevated levels of liver aldolase B (D) a deficiency of liver hexokinase 13. Which one of the following is the major end product of protein-Nitrogen metabolism ? (A) Glycine (B) Uri ...
103 topic summary
103 topic summary

... Denaturation of proteins: heat, acids and bases, organic compounds, heavy metal ions and agitation Chapter 21: Enzymes as catalysts (effects on activation energy and reaction rates) Classification of enzymes: names, substrates and type of reaction catalyzed Enzyme specificity: active site, substrate ...
File - Biology with Radjewski
File - Biology with Radjewski

...  Pyruvate converts to acetaldehyde and then is reduced to ethanol.  It uses enzymes at both steps  Two molecules of CO2 and 2 ATP are produced in this anaerobic pathway ...
Taken from http://www.gtac.edu.au/ 2007 EXPLORING ENZYME
Taken from http://www.gtac.edu.au/ 2007 EXPLORING ENZYME

... 10. How can all of these amino acids be associated with the carbohydrate molecule when they are so far apart in the primary structure (amino acid sequence) of this protein? ...
MC 2
MC 2

... 5. All enzymes function optimally across a very narrow range of pH. When the pH strays beyond this range, the shape of the protein changes, which is a process called denaturing. Even a small change in shape to the active site can drastically affect its ability to bind to the substrate. 6. All organi ...
GENE to PROTEIN
GENE to PROTEIN

... • First codon decipher was UUU • There are 64 codons • A codon codes for only 1 amino acid The genetic code must have evolved very early in the history of life because it is nearly universal among living organisms. ...
GENE to PROTEIN
GENE to PROTEIN

... • First codon decipher was UUU • There are 64 codons • A codon codes for only 1 amino acid The genetic code must have evolved very early in the history of life because it is nearly universal among living organisms. ...
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... aid in blood clotting, build hair and nails, suport body tissues, break apart food molecules, allow muscles to contract, and participate in countless other processes. *Illness and death can result if even one type of protein is missing! ...
Mutations Lab
Mutations Lab

... based on whether they are hydrophobic, hydrophilic, or if they are cysteine amino acids (which will form disulfide bonds). You will then fold your chain of amino acids/strip of paper into a specific shape based on these properties (you can tape or staple your cysteine amino acids together to create ...
NATURE`S BIOLOGICAL BUILDING BLOCKS
NATURE`S BIOLOGICAL BUILDING BLOCKS

... Composition: mostly carbon and hydrogen with some oxygen Includes fatty, greasy and waxy compounds relatively insoluble in water, but soluble in organic solvents such as ether and benzene. Neutral Fats - high energy molecules consisting of glycerol and fatty acids. Phospholipids - neutral fat with o ...
Amino acids - Workforce3One
Amino acids - Workforce3One

... -carbon bonded to carbon, or -carbon bonded to other molecules. • Carbon can form up to 4 covalent bonds. • Carbon may be bonded to functional groups with specific properties ...
Biological Molecules
Biological Molecules

... nucleotides side-byside. What is the type of bond that forms the cross-links holding the two strands together? ...
Organic Molecules
Organic Molecules

... • Phospholipids a. lecithin (phosphatidylcholine) ...
Biochemistry: Monomers and Polymers
Biochemistry: Monomers and Polymers

... Def. of Amino Acid • Amino acids are molecules that contain C, H, O, N, and sometimes sulfur. – Our bodies are able to make 12 of the 20 amino acids, the rest come from what you eat. – The amino acid monomers are linked together by peptide bonds to form protein polymers. ...
Biomolecules - Good Earth School
Biomolecules - Good Earth School

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Structure of proteins Insulin:

1 Which of the following are the smallest cells? A) human ovum B
1 Which of the following are the smallest cells? A) human ovum B

... DNA sequence ...
ppt file/carboxilase
ppt file/carboxilase

... membrane potential is disrupted, mitochondrial structural abnormalities occur. c.) in brain the astrocytes produce glutamine from glutamate, that is derived from a-ketoglutarate. It withraws CAC intermediate. Glutamine is taken up and transformed to glutamate in neurons. Glutamate is the main stimul ...
polar charged phosphate head and nonpolar uncharged fatty acid
polar charged phosphate head and nonpolar uncharged fatty acid

... Large polymer made of repeating monomers called amino acids A. Functions of Proteins ...
Organic Chemistry
Organic Chemistry

... Proteins: the basis of life diversity • Proteins are a class of diverse macromolecules that determine many characteristics of cells and, in turn, of the whole organisms. • All proteins are polymers constructed of subunits called amino acids. There are 20 types of amino acids in protein. Thus, the bi ...
Glycolysis Embden-Meyerhoff pathway
Glycolysis Embden-Meyerhoff pathway

... Pyruvate end product effect of aresenate ...
Translation
Translation

... Initiation results in the formation of an initiation complex in which the ribosome is bound to the specific initiation (start) site on the mRNA while the initiator tRNA charged with (Nformyl)methionine is annealed to the initiator codon and bound to the ribosome. - Protein synthesis begins with a AU ...
Document
Document

... high temperatures. However, the abiodic formation of amino acids requires NH3 • NH3 was not stable in the Archean atmosphere ...
< 1 ... 539 540 541 542 543 544 545 546 547 ... 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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