Biochemistry + Nutrition:

Carbon compounds are also known as organic compounds . Therefore anything that bonds with a carbon is an organic compound Carbon Compounds can form 4 covalent bonds 4 single bonds 2 double bonds 1 triple bond + 1 single bond

Covalent bond: when atoms of a molecule share electrons Ionic Bond: bond in which one or more electrons from one atom are removed and attached to another atom, resulting in positive and negative ions which attract each other. One extra electron is given to an atom that needs one electron to complete it.

An electron shell is the shell that is outside the proton and neutron. It needs 2 electrons on the first shell It needs 8 electrons on the second shell It needs 8 electrons on the third shell -Number of Protons = Atomic Number -Number of Electrons = Number of Protons = Atomic Number -Number of Neutrons = Mass Number - Atomic Number

Key Functional Groups Functional groups give molecules unique properties Hydroxyl group (-OH) found in alcohols helps molecules dissolve in water Amine group (-NH2) found in amino acids Carboxyl group (-COOH) found in amino acids and in fatty acids (a type of lipid) makes molecules acidic

Key Definitions in Biochemistry: Monomers- building blocks of polymers o Monomers are also the smallest units. (animo acids) Hydrolysis- breaking down two monomers in a polymer by giving back a water molecule Dehydration Synthesis- the formation of a polymer by taking out a water molecule and fusing two monomers Condensation Reaction Dehydration Synthesis Joining two monomers to create a polymer Removes a water molecule OH from one monomer H from the other monomer

Monomer + Monomer

Dipeptide + H20

Condensation Reaction Hydrolysis Breaking apart a polymer by adding back in a water molecule One monomer receives OH The other monomer receives H Sucrose + H20 Glucose + Fructose

Organic Molecules Carbohydrates Primary source of energy for living things (sugars) Plants use carbs for structural support Short term energy storage -Lipids Long term storage of energy Used in cell membranes Waterproof (hydrophobic)

Proteins Enzymes catalyze chemical reactions Proteins found in Muscles, bones, gateways into cells Nucleic Acids Genetic information is encoded in nucleic acids

Carbohydrates General characteristics C:H:O in a 1:2:1 ratio in their simplest form (monosaccharides) Groupings Monosaccharides, such as glucose and fructose (C6H12O6) Disaccharides, such as sucrose (table sugar) glucose + fructose = sucrose Polysaccharides, such as starch (plants), glycogen (animals), cellulose (plants)

Lipids General Characteristics Nonpolar so are hydrophobic (don t dissolve in water) Store energy in the many C-H bonds Saturated fats (solids at room temp) and unsaturated fats (liquid at room temp) Ex. Chlorophyll is a pigment used in photosynthesis Fatty Acids Long C-H chains Store lots of energy Building block for other lipids Lipids Phospholipids Cell membranesbilayer Two fatty acids + glycerol + polar head Hydrophilic head Hydrophobic tails Lipids Triglycerides -Three fatty acids + glycerol

Review Questions General Biochem, Carbs, Lipids 1. What element do all organic compounds have?

2. Name the 4 types of organic macromolecule studied in biochemistry.

3. What three shapes do organic compounds commonly take?

4. Many monomers put together are called what?

5. What type of chemical reaction creates polymers?

6. What type of chemical reaction can break apart polymers using water?

7. Give an example of a monosaccharide (simple carbohydrate)?

8. Give an example of a lipid and how/where it is used.

Proteins Proteins are made from chains of amino acids 20 different amino acids are used Amino acids are joined via dehydration synthesis to create peptide bonds (a covalent bond), and polypeptide chains These chains are then folded to create the 3D structure of a protein

Function of Proteins Muscle Mass Collagen (protein in skin, ligaments, tendons) Antibodies (part of immune system) Hemoglobin (carries oxygen in blood) Enzymes (catalyze chemical reactions)

Binding Specificity
Even when different substrate molecules are present, only those that have the specific shape complementary to the active site are able to bind with the enzyme's active site.

Enzyme Structure
Enzymes are globular proteins. Their folded conformation creates an area known as the active site. The nature and arrangement of amino acids in the active site make it specific for only one type of substrate.

Temperature and Enzyme Function

Chemical reactions speed up as temperature is increased, so, in general, catalysis will increase at higher temperatures. However, each enzyme has a temperature optimum, and beyond this point the enzyme's functional shape is lost. Boiling temperatures will denature most enzymes.