Are you what you eat?

1. The important Characteristics of Carbon Forms 4 covalent bondsForms double and triple bondsForms long chains and ringsCan bind with many other elementsEven electron distribution (nonpolar

molecules)

2. Macromolecules, Monomers and Polymers(Hint: think of the meaning of the prefixes)

What do these words mean?

Polygons

Polygamy

Polyester

2. Macromolecules, Monomers and Polymers

Polymer – Smaller organic molecules join into long chains.

Monomer – the individual unit that builds up polymers

Macromolecules – Very large molecules

3. Dehydration synthesis and HydrolysisThese two terms refer to the processes that

forms monomers and polymers:Dehydration synthesis – A reaction that

removes molecules of water to form polymers from monomers

Hydrolysis – The reaction that adds water to polymers to separate them to their individual monomers.

(http://nhscience.lonestar.edu/biol/dehydrat/dehydrat.html or http://www.youtube.com/watch?v=UyDnnD3fMaU )

IsomersMolecules that have the same formula, but

different structures.Examples: Glucose and Fructose

4. What are the big four?

Three out of the 4 types of biochemical macromolecules can be found on food nutrition labels…

Look at the label to the left. 3 of the 4 macromolecules can be found in foods.

1____________________

2____________________

3____________________

(0 grams in this product)

(13 grams in this product)

(9 grams in this product)

4. What are the big four?Fats (we call them lipids)CarbohydratesProteins Nucleic acids (DNA and RNA)

When studying these biochemical molecules, we are interested in finding out…..

what they do for living things.what they generally look like.what their monomers are.and how they may help the body gain

energy to sustain life.

SO, LETS GET STARTED!

Great website for reference…http://biomodel.uah.es/en/model3/

index.htm

5. CarbohydratesMolecules that form from atoms in C1:H2:O1 ratioMonomers: Monosaccharides (simple sugars)Monosaccharides are usually sweet, white powdery

substances (such as fructose, glucose) that form rings of carbon atoms.

Monosaccharides in general serve as direct, quick sources of energy for living organisms during cellular respiration, they are building blocks of many polymers

Important monosaccharides:GlucoseFructose

Disaccharides – two monosaccharide molecules combine by dehydration synthesis to form disaccharides

Important disaccharides: Lactose – found in milk sugarSucrose – table sugar

Polysaccharides – many (tens to hundreds) units of monosaccharides combine by dehydration synthesis

Polysaccharides also separate to monosaccharides by hydrolysis while taking in water.

Important polysaccharides:Starch – made up of many glucose units, it is an

important storage polysaccharide that is found in plant roots and other tissues. It stores monosaccharides that can be broken down later to release useful energy during cellular respiration – ONLY IN PLANTS

Glycogen – also made up of many glucose units, it is an important storage polysaccharide in the liver and animal muscles. It can also be broken down to monomers to release energy during cellular respiration. ONLY IN ANIMALS

Cellulose – also made up of many glucose units. However, in this case the molecule is not easily broken down to its monomers. It is important for providing a rigid structure in plant cell walls.

Chitin – made up of some nitrogen containing monosaccharides. It is an important polysaccharide that provide the solid structure of arthropods and fungi.

6. Lipids a diverse group of molecules that are nonpolar

and generally do not dissolve in waterThey mostly contain carbon, hydrogen, very few

oxygen atoms, but some also have phosphorous.There are three distinct groups of lipids:

Simple lipidsPhospholipidsSterols

6A. Simple LipidsVery large molecules that form from 2 different

kinds of monomers by dehydration synthesis:3 Fatty acids – are long chains of carbon with

oxygen at the end (can be saturated and unsaturated)

1 Glycerol – smaller 3-carbon compound.

Simple lipids are important as storage materials in all living things. They can store twice as much energy as polysaccharides can.

Fatty tissue cushions vital organs and insulates the body.

Plant fats contain more unsaturated fatty acids, while animal fats contain more saturated fatty acids.

Simple lipids also dissolve vitamins http://biomodel.uah.es/en/model3/index.htm

6B. PhospholipidsPhospholipids – phosphate containing lipids.Their monomers: 1 glycerol + 2 fatty acids

(saturated and unsaturated) + phosphate. These monomers combine by dehydration synthesis

Phospholipids have both polar and nonpolar sections. As a result, they are able to dissolve in both type of solvents as well.

They are important for living things because they form the borders of all cells (cell membranes) and also participate in forming many cell organelles.

6C. STEROLSSterols are a highly nonpolar (hydrophobic)

group of molecules. They occur naturally in plants, animals, and

fungi, with the most familiar type of animal sterol being cholesterol.

Cholesterol is vital to cellular function, and a precursor to fat-soluble vitamins and steroid hormones.

3-six sided rings and one 5-sided ring + alcohol

7. ProteinsProtein- Polymer constructed from amino

acid monomers. Only 20 amino acids, but make 1,000s of

proteinsSome are 100 a.a. in length; some are

thousands3-D Protein

7A. Protein FunctionsEach of our 1,000s of proteins has a unique 3-D

shape that corresponds to a specific function: Defensive proteins

Antibodies in your immune system Signal proteins

Hormones and other messengers Hemoglobin

Delivers 02 to working muscles Transport proteins

Move sugar molecules into cells for energy (insulin) Storage proteins

Ovalbumin (found in egg white) used as a source of amino acid for developing embryos

Most important roles is as enzymes Chemical catalysts that speed and regulate virtually all chemical

reactions in cells Example, lactase

7B. Amino Acid structureProteins diversity is based on differing

arrangements of 20 amino acids. Amino acids all have an amino group and a carboxyl

group. R group is the variable part of the amino acid;

determine the specific properties of the 20 amino acids.

Two main types: Hydrophobic

Example: Leucine R group is nonpolar and hydrophobic

Hydrophilic Polar and charged a.a.’s help proteins dissolve in aqueous

solutions inside cells. Example: Serine

R group is a hydroxl group

7C. Amino Acid DehydrationCells join amino acids together in a

dehydration reaction:Links the carboxyl group of one amino acid to

the amino group of the next amino acid as a water molecule is removed.

Form a covalent linkage called a peptide bond making a polypeptide.

7D. Protein StructurePrimary Structure

Unique sequence of amino acidsFor any protein to perform its specific function,

it must have the correct collection of amino acids arranged in a precise order. Example: a single amino acid change in hemoglobin

causes sickle-cell disease Determined by inherited genetic information.

7D. Protein StructureSecondary Structure

Parts of the polypeptide coil or fold into local patterns. Patterns are maintained by regularly spaced hydrogen

bonds between the hydrogens of the amino group and the oxygen of the carboxyl groups.

Coiling results in an alpha helix. Many fibrous proteins have the alpha structure over

most of their length Example: structural protein of hair

Folding leads to a pleated sheet. Make up the core of many globular proteins Dominate some fibrous proteins, including the silk

proteins of a spider’s web

7D. Protein Structure

7D. Protein StructureTertiary Structure

Overall, three-dimensional shape of a polypeptide.

Roughly describe as either globular or fibrousGenerally results from interactions among the R

groups of amino acids making up the polypeptide.

7D. Protein StructureQuaternary Structure

Results from association of subunits between two or more polypeptide chains.

Does not form in every protein.Example, Hemoglobin

8. Nucleic AcidsTwo types:

DNA and RNA

8 A. DNADeoxyribonucleic Acid (DNA)

Monomers made up of nucleotides: Nucleotides consist of:

A five carbon sugar, deoxyribose Phosphate group Nitrogenous base (Adenine, Guanine, Cytosine,

Thymine)

8A. DNA As a Polymer, DNA is a…Double helix consists of:

Sugar-phosphate backbone held by covalent bonds Nitrogen bases are hydrogen bonded together; A

pairs with T and C pairs with G

8A. DNA Consists of genetic material that organisms

inherit from their parents.Made up of genes:

Specific stretches of DNA that program amino acid sequences of proteins.

8B. RNAAlso made up of monomers of nucleotides

Nucleotide of RNA: Sugar is ribose (not deoxyribose) Phosphate group Nitrogen bases (Adenine, Uracil (instead of

Thymine, Guanine, and Cytosine)

8B. RNAServes as a intermediary for making proteinsConsists of a single-strand

10. EnzymesEnzymes are proteins that act as biological

catalysts in living organisms.They speed up chemical reactions by lowering

the activation energy of the reaction.

http://www.stolaf.edu/people/giannini/flashanimat/enzymes/transition%20state.swf

10A. Enzyme SpecificityEnzymes have a specific section called the

active site that is able to bind with the reactants (substrates) of a chemical reaction

Once the substrates bind to the active site, the active site changes shape and pulls the reactants together. As a result, the reaction occurs faster and more efficiently.

The model that describes that enzymes change shape when bind with the substrate is called the induced fit model

10B. Induced Fit Model

Animations: http://highered.mcgraw-hill.com/sites/0072495855/student_view0/chapter2/animation__how_enzymes_work.html

http://www.lpscience.fatcow.com/jwanamaker/animations/Enzyme%20activity.html

http://www.northland.cc.mn.us/biology/biology1111/animations/enzyme.swf

10C. Enzyme CharacteristicsThree important special characteristics of

enzymes:They are specificThey are efficientThey are sensitive

10D. Cofactors and InhibitorsCofactors:

Many enzyme do not function without an additional group attached to them. This additional group is called a cofactor.

Inhibitors:Some substances can stop enzymes from

functioning by attaching themselves to the active site of the enzyme. These are called inhibitors.

Many inhibitors are used as poisons or drugs.