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Macromolecules

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Latifah Tilus

on 12 November 2014

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Transcript of Macromolecules

• Textbook
• http://www.healthaliciousness.com/articles/foods-highest-in-protein.php
• http://www.choosemyplate.gov/food-groups/protein-foods.html
• http://www.agriinfo.in/default.aspx?page=topic&superid=4&topicid=1576
• http://healthyeating.sfgate.com/eight-types-protein-function-4559.html
• http://www.daviddarling.info/encyclopedia/F/fibprot.html
• http://www.daviddarling.info/encyclopedia/G/globprot.html
Proteins
Macromolecules
Macromolecules
Very large organic molecules, usually polymers, composed of hundreds or thousands of atoms
Lipids
Proteins
Nucleic Acids
*There are 2 types of nucleic acids
deoxyribonucleic acid or DNA
ribonucleic acid or RNA

*Nucleic acids are the molecules that code the genetic information of organisms

*The 2 acids are used in repair, reproduction and protein synthesis.
DNA and RNA are polymers made up of monomers called nucleotides
Carbohydrates
Organic compounds containing carbon, hydrogen, and oxygen
Exist as
monosaccharides, disaccharides, and polysaccharides
Used for structural material and as sources of energy
Monosaccharides
Simple sugars containing carbon, hydrogen, and oxygen
Common monosaccharides: glucose, fructose, and galactose
Share the same chemical formula but have different physical properties
Sources of Proteins
Properties and Functions
Properties:
Optical Property
Colloidal
Solubility
Amphoteric Nature
Denaturation of Proteins
DNA
*Macromolecules

*Shaped like a twisted double helix and is composed of long strands of altering sugars and phosphate groups

*Has nitrogenous bases (adenine, thymine, guanine and cytosine)

*Contains the genetic information necessary for the production of other cell components and for the reproduction of life
RNA
*Composed of nucleotides

*Plays a major role in protein synthesis

*Involved in the decoding, transcription and translation of the genetic code to produce proteins

*Nucleotides contain 3 components
-Nitrogenous base
-5 carbon sugar
-Phosphate group
William Ruiz
Any class of nitrogenous, organic compounds that consist of large molecules composed of one or more long chains of amino acids and are an essential part of all living organisms. They are composed mainly of carbon, hydrogen, oxygen, and nitrogen.
They make up horns, hair, muscles, and many biological catalysts.
Many proteins are formed by a linkage of monomers called amino acids.
R groups give proteins different shapes, which allow proteins to carry out many different activities in living things.
Proteins are composed of one or more polypeptides, making some proteins very large molecules, containing hundreds of amino acids.
Often long proteins, such as those, are bent and fold as a result of reactions, such as hydrogen bonding between individual amino acids
Protein shape can also be affected by conditions, such as temperature and the type of solvent in which the protein is dissolved.
Subgroups of proteins are fibrous and globular proteins.
Functions:
Storage
Transport
Structural Material
Metabolic Growth Regulator
Control of Physiological Functions
Catalytic Activity
Hormonal
Toxicity of Foreign Proteins
By: Julie Fan
Disaccharides
Polysaccharides
Meats
Beef
Ham
Lamb
Pork
Veal
Bison
Rabbit
Venison
Poultry
Chicken*
Turkey*
Duck
Goose
*Primarily the breast
Seafood
Tuna
Salmon
Halibut
Catfish
Cod
Flounder
Haddock
Herring
Mackerel
Pollock
Porgy
Sea Bass
Snapper
Swordfish
Trout
Clams
Crab
Crayfish
Lobster
Mussels
Octopus
Oysters
Scallops
Squid (calamari)
Shrimp
Others
Tofu
Cheese*
Beans
Eggs
Milk
Yogurt
Soymilk
Tempeh
Beans and Peas*
Nuts and Seeds*

*Mozzerella a.nd Cottage Cheese
*Black beans, Lima beans, Soy beans,
split peas, etc.
*Almonds, Cashews, Peanuts,
Pumpkin, Sesame, Sunflower,
Watermelon Seeds, etc.
Glucose
Fructose
Galactose
(fuel for cells)
Amino Acids
There are 20 different types of amino acids, which all share a basic structure.
All amino acids contain a central carbon atom, covalently bonded to 4 other atoms or functional groups.
The main difference between the different amino acids is the R group. (R group can be complex or simple)
Amino acids are c0mmonly in a simplified way such as balls.
Two amino acids bond to form a dipeptide. This bond is known as a peptide bond, and release a water molecule.
Amino acids often bond to form long chains called polypeptides.
About half of the energy used by the body is provided by glucose
Functions:
Respiration
Heart regulation
Muscle contraction/relaxation
Temperature regulation
- A single hydrogen bonds at one site
- A carboxyl group, -COOH, bonds at another
- A amino group, -NH2, bonds at a third site.
- A side chain, R group, bonds at a fourth site.
found in produce, grains, and foods with added sugar:
jam/jelly
canned fruit
dried/candied fruits and vegetables
oatmeal
granola
**Monique Bergeron**
Has a sweet taste
Sucrose
(sugar): reactant of fructose and glucose
Functions:
Producing energy
Storing energy
found in healthy/ nonhealthy foods:
High in fructose:
Pineapple
Blackberries
Raspberries
Blueberries (very high)
Low in fructose:
Avocado
Lime
Lemon
Enzymes
Enzymes are RNA or protein molecules that act as biological catalysts.
They are essential for the functioning of any cell.
Many enzymes are proteins.
Enzyme reactions depend on a physical fit between the enzyme molecule and its specific substrate, the reactant being catalyzed.
Enzymes have folds known as an active site, with a shape that allows the substrate to fit in.
An enzyme only works on a specific substrate because only that substrate fits into the active site.
The linking of an enzyme and its substrate cause the shape of the enzyme to change, which weaken chemical bonds in the substrate, reducing its activation energy
Because the enzyme itself is unchanged, it can be used many times.
After the reaction, the enzyme releases the products
An enzyme may not work if its environment is changed, such cases being a change in temperature or pH, which causes the shape of the enzyme and substrate to change.
If such a change occurs, the reaction that the enzyme would have catalyzed cannot happen.
Enzyme Reaction
Stored in the form of
glycogen
in organisms
Glycogen:
consisting of hundreds of glucose molecules stuck together in a complex chain
Glucose is stored in the form of the polysaccharide
starch
for plants
Starch:
Two basic forms, either in highly-branched chains or long, unbranched ones
Reacts with glucose to make
lactose
Functions:
A fundamental & structural substance for cells and cell walls
Can be found in milk, whey, and the human body
(composed of three or more monosaccharides)
Plants also produce the polysaccharide
cellulose
Cellulose:
gives plants strength and stiffness
Thousands of glucose monomers in cellulose molecules create long, straight links that can be broken down by hydrolysis
Two monosaccharides that combine (in a condensation reaction) to make a double sugar (disaccharides)
Three most important disaccharides:
sucrose, lactose, and maltose
Sucrose
Lactose
Maltose
(Non-reducing sugar)
(Reducing sugar)
(Reducing sugar)
Works Cited/Resources
(textbook)
www.rsc.org/education/teachers/resources/cbf/carbohydrates.htm
www.galactose.org
Carbohydrates
Optical Property- absorption of light at higher energies due to the surface structure, composition, and topography of the surface of a protein molecule.
Colloidal- finely divided particles are dispersed in continuous medium in a way that prevents the particle from filtering easily or settling rapidly
Solubility- the solubility of the protein depends on the pH of the solvent.
Amphoteric Nature- able to react as both an acid and a base according to the pH of their surroundings.
Denaturation of Proteins- changes in the solubility of individual protein molecules due to change in structure when exposed to heat resulting in the entrapment of solvent water in a semi-solid gel structure. (like in gelatin)
Storage- stores mineral ions such as potassium and iron, and regulates and guards against effects on the body.
Transport- carries vital materials like oxygen to cells in the body.
Structural- forms the connective framework of the muscles, bones, tendons, skin, and cartilage. Also, proteins are the main structural components in hair, nails, teeth and skin.
Metabolic Growth Regulator- regulates metabolic processes in the cells, including liver functions, stomach digestion, blood clotting, and converting glycogen to glucose.
Control of Physiological Functions- regulates the strength and speed of heart and muscle contractions, absorption of calcium from the intestinal walls, and stimulates endocrine glands to secrete epinephrine and insulin to regulate blood sugar levels, etc.
Catalytic Activity- reducing required activation energy in foods.
Hormonal- hormones are protein-based chemicals usually transported through the blood, and act as chemical messengers that transmit signals from one cell to another.
Toxicity of Foreign Proteins- found in antibodies and attacks bacteria and foreign invaders to render them inactive.
http://www.chem4kids.com/files/bio_lipids.html
http://dictionary.reference.com/browse/lipid?s=t

Lipids
Monosaccharide:
a-glucose + a-fructose
Monosaccharride:
a-glucose + a-glucose
Monosaccharide:
a-glucose + b-galactose
(CH3)
any of a group of organic compounds that are greasy to the touch, insoluble in water, and soluble in alcohol and ether
Nucleic Acids
Complex Carbohydrates: (complex chains)
Apples
Brown rice
Carrots
Low-fat yogurt
Multi-grain bread
http://biology.about.com/od/molecularbiology/a/nucleicacids.htm
http://www.chem4kids.com/files/bio_nucleicacids.html
Simple Carbohydrates: (simple chains)
Honey
2% or regular milk
Cereal
Table sugar
Jams
Fruit juice
Triglycerides
Contains hydrogen, oxygen, and carbon

Fibrous And Globular Proteins
Fribrous protiens are proteins that possess an extended, fiber-like structure and are important structural building-blocks.
Fribrous proteins can be broken down into keratins, collagens, a elastins.
Globular proteins are compact, vaguely spherical-shaped proteins, which include all non-structural types of proteins.
Globular proteins either are or are key components of enzymes, hormones, antibodies, and some structural proteins.
Keratins- an insoluble, sulfur-containing fibrous protein, which makes up hair, fingernails, and bird feathers.

Collagens- the fibrous protein that is the main component connective tissue. It can be found in tendons, skin, bone, cartilage, and ligaments.

Elastins- a fibrous protein that coils and recoils like a spring within the elastic fibers of connective tissue. It is responsible for the elasticity of the skin, blood vessels, heart, lungs, intestines, tendons, and ligaments
Enzymes- biological catalysts with about 1,000 different varieties found in the human body.

Hormones- any substance that is produced in tiny amounts in one part of an organism and then transported to other parts where it has a physiological effect. They control the rate at which reactions proceed.

Antibodies- a special kind of blood protein secreted by B-lymphocytes, a type of white blood cell in the immune system. They circulate in the bloodstream to attack any foreign substances.

Structural Proteins- globular proteins form part of the cell membrane, which has a structural role and a role in transporting ions in and out a cell.
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