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BIOMOLECULES
BIOMOLECULES

... Remember: Elements are C, H, O, and N “R” groups represent one of the 20 Amino Acids! (so, each amino acid has something different in that spot) ...
DNA, RNA, Protein Graphic Organizer
DNA, RNA, Protein Graphic Organizer

... Sickle Cell DNA/RNA Mutation Worksheet Sickle cell anemia is a disease that is passed down through families. Normal red blood cells are shaped like a disc, while sickle blood cells are shaped in a crescent shape. Sickle cell anemia is caused by an abnormal type of hemoglobin. Hemoglobin helps carry ...
Organic Macromolecules
Organic Macromolecules

... Read Chapter 3 in your book and fill out this graphic organizer. You will use this when you do your Macromolecule Flapbook. Organic Molecule Simple Carbohydrate ...
10 DNA Vocabulary - Petal School District
10 DNA Vocabulary - Petal School District

Handout12B
Handout12B

Non Oxidative deamination
Non Oxidative deamination

... Some amino acids can be deaminated to liberate NH4 without oxidation. Serine, homoserine and threonine , they undergo deamination catalysed by the enzyme dehydratase with pyridoxal phosphate as a coenzyme. ...
hwk- pg-331 - WordPress.com
hwk- pg-331 - WordPress.com

Protein Synthesis - Helena High School
Protein Synthesis - Helena High School

... 8. What is the job of helicase in transcription? 9. What are the two jobs or RNA polymerase in transcription? and 10. What is the goal of translation? 11. In eukaryotic cells translation happens in what location of the cell? structure? ...
File - Biology Class With Mrs. Caskey
File - Biology Class With Mrs. Caskey

... ____________________ 5. This is the name given to an amino acid added to a dipeptide. ____________________ 6. Of what kind of organic compound are oils, waxes, and fats an example? ____________________ 7. These are the individual subunits that make up DNA and RNA. ____________________ 8. What is a l ...
Click here to go back
Click here to go back

... binds to a ribosome  tRNA carries an amino acid to the ribosome ...
Nutrients and the structure of macromolecules File
Nutrients and the structure of macromolecules File

... OH R There are 20 naturally occurring amino acids. The “R” group is the only part of the amino acid that makes them different from one another. It is the combination and number of these 20 amino acids in proteins that gives us our varying traits. When peptide bonds hook amino acids together into a c ...
Ch. 4-5 - Carbon and Organic Chem
Ch. 4-5 - Carbon and Organic Chem

... Tertiary structure – disulfide bridges, ionic bonding, or h-bonding of R-groups ...
organic molecules : proteins - Mr. Lesiuk
organic molecules : proteins - Mr. Lesiuk

... ________________________________________________________________________ ________________________________________________________________________ - New bonds can form to hold it into a three-dimensional shape. Three types of bonds are involved in this structure: ionic, covalent and/or hydrogen. ____ ...
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... __29. Cholesterol is the base molecule that will form which product? a. hormones ...
Secondary structure
Secondary structure

... • A few amino acids in a chain are called a polypeptide. A protein is usually composed of 50 to 400+ amino acids. • Since part of the amino acid is lost during dehydration synthesis, we call the units of a protein amino acid residues. carbonyl carbon ...
Main concepts Carbohydrates Fats, Proteins and Enzymes
Main concepts Carbohydrates Fats, Proteins and Enzymes

... 21. Proteins perform many roles in a healthy functioning body. Fibrous proteins provide structure for many body components eg hair, skin, tendon and cartilage; globular proteins transport oxygen, function as antibodies that fight disease and catalyse biochemical reactions. 22. Proteins are large bio ...
What is Biotechnology?
What is Biotechnology?

... Alcohol: top fermentation, bottom fermentation.  Vinegar: microorganisms oxidize wine.  Commercial products, eg. glycerol, acetone,butanol, lactic acid, citric acid, yeast biomass ...
One gene
One gene

... temperatures (permissive temperature). The mutation results in a slight destabilization and alteration of the 3D conformation of the enzyme An example of a TS mutation: Dogs and cats that are white with black feet or vice versa The gene for coat color is normal at cold temperatures The extremities a ...
FERMENTATION: an anaerobic biological reaction process in which
FERMENTATION: an anaerobic biological reaction process in which

... Important ponts: • the small molecule is called an effector or a modulator • if the allosteric interaction involves an enzyme the modulator binds at a site other than the active site • the modulator can activate or inactivate a protein ...
The Chemistry of Life
The Chemistry of Life

... making energy (ATP)  for synthesis, growth & everyday functions ...
Alcoholic fermentation
Alcoholic fermentation

... 13a) How does a cell use feedback inhibition to control its catabolism? As ATP concentration decreases, respiration speeds up; as ATP concentration increases, respiration slows down (regulated by enzymes) 13b) What is the role of the enzyme phosphofructokinase in this feedback inhibition? It catalyz ...
MACROMOLECULE SUMMARY SHEET
MACROMOLECULE SUMMARY SHEET

... Examples ...
biochem 38 [4-20
biochem 38 [4-20

... What is the major process for removing nitrogen from amino acids called? Which amino acids cannot undergo this process?  Transamination is the major process which removes nitrogen from AAs  Lysine and threonine cannot undergo transamination ...
Slide 1
Slide 1

...  Uncoil protein’s strands  Enzymes attack peptide bonds ...
Introduction- Amino acid protection and deprotection is particularly
Introduction- Amino acid protection and deprotection is particularly

... amino acid ester (2). Amino acid protection and deprotection is also used in peptide synthesis of amino acid in solid and solution phase synthesis , the advantage of solution phase synthesis is to isolate and characterized at every step(3) An alpha-amino acid has the generic formula H2NCHRCOOH, wher ...
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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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