Chapter 3 Hydrocarbon Methane Ethane Propane Butane Pentane Hexane Haptane Octane Nonane Decane Molecular Formula CH4

C2H6 C3H8 C4H10 C5H12 C6H14 C7H16 C8H18 C9H20 C10H22 # of Carbons 1 2 3 4 5 6 7 8 9 10 # of Hydrogen 4 6 8 10 12 14 16 18 20 22

Hydrocarbon Formulas Single Bond- CnH2n+2 , :ane Double Bond- CnH2n , :ene Triple Bond- CnH2n-2, :yne Isomers- Compounds that same the same molecular formula but different structures 3 types of Isomers Structural- Different in Covalent arrangement Geometric- Identical bonds but different order in which groups are arranged Enantiomers Mirror images

Functional Groups Hydroxyl-Alcohols, -OH Carbonyl-Ketones, CO Carboxyl- Acidic, COOH Amino- Amide, Basic NH2 Phosphate- Acidic, ATP, PO4 Sulfhydryl Thiols, Cysteine, SH

MacroMolecules Monomer Dimer- 2 Monomers Polymers produced by the linking of small organic compounds (monomers)

Polymer (Macromolecule)

Make (dehydrate) loses H2O, Condensation Reaction Break (hydrate) Gains H2O, Hydrolysis Reaction

Carbohydrates A sacharide is the carbohydrate version of a monomer 1 sugar unit: Monosacharide 2 sugar units: Disacharide More than 2 sugar units: Polysacharide

Glucose- most abundant monosaccharide, helps maintain blood sugar (homeostatic)

Trioses

Dihydroxyacetone Ribose

Monosacharides

Carbs:

Disacharides

Deoxyribose Glucose Hexose Fructose Galactose Glycosidic linkage Maltose: Glucose+ Glucose Sucrose: Glucose+ Fructose Lactose: Glucose+ Galactose

Pentose

Polysacharides Starch Glycogen Cellulose Beta Glucose

Alpha Glucose Starch

Starch- Energy in plants Glycogen- Short term energy in animals Cellulose- Gives plants their structure

Starch is a polymer consisting of Alpha-Glucose subunits Cellulose is the most abundant carb, Gives plants their structure, Beta-Glucose

Special Carbs Amino Sugars- glucosamine & galactosamine Chitin-Component of external skeleton of arthropods, Calcium Carbonate makes it harder, polymer of Glucose + amino acid Glycoproteins- proteins secreted by cells Glycolipids- recognition compounds on surfaces of animal cells

Glycoproteins and Glycolipids are found in the cell walls/membranes and help the immune system. In Alpha the OH is below the carbon In Beta the OH is above the carbon

Lipids Fats (solid) single bond, (saturated fats) BAD Lipids Oils (liquid) double or triple bond ( unsaturated fats) GOOD

Wax Candles

Steroids Medicine

Phospholipids Plasma Membrane

Lipids- composed of 3 acids & 1 glycerol Phospholipids- (amphipathic) Make up the phospholipid bi-layer, have a hydrophobic end and hydrophilic end. Composed of 2 fatty acids + glycerol + phosphate. Caratenoids- yellow and orange pigments Steroids have fused carbon rings + Functional group Waxes-long chain of fatty acids + long chain of alcohols, Water proof, resist degradation, forms protective covering Prostoglandis- Chemical mediators

Proteins Composed of amino acids in peptide bonds Distributions and amounts of proteins determine what the cell looks like and how it functions Most enzymes are proteins Enzymes-accelerate chemical reactions

Amino Acids in Proteins Sub-units of proteins Have an amino group NH2 & Carboxyl group COOH, bonded to an alpha carbon (COOH) donates a proton and becomes charged (NH2) accepts an proton and becomes + charged

20 essential amino acids found in most proteins, identified by a variable side chain (R group) bonded to the Alpha carbon

Amino acids are group by the properties of their side chains Nonpolar- side chains are Hydrophobic Polar- side chains are Hydrophilic Side chain with carboxyl group are Acidic Side chain that accepts a Hydrogen ion is Basic

Protein (a a-): (a a-) + (a a-)

peptide bond. More than 2 bonds is a polypeptide

Hydrophobic Hydrophilic Basic Acidic Proline Serine Lysine Glutamic

(a a-) = Amino Acids Essential Amino Acids Amino Acids an animal cant synthesize in amounts sufficient to meet its needs and must obtain them through its diet. 9 essential Amino Acids for Adult Humans(memorize) Isoleucine Leucine Lysine Methionine Phenylalanine Threonine Tryptophan Valine Histidine

Peptide Bonds Amino acids combine chemically by a condensation reaction b/w the Carboxyl group of one amino acid and the amino nitrogen of another amino acid

2 amino acids join to form a dipeptide More than 2 create polypeptide

Peptide bond Covalent carbon-to-nitrogen bond linking 2 amino acids

4 levels of Protein Organization Primary- The sequence of amino acids in a polypeptide chain, specified by instructions in a gene Secondary- a-helix- H-bonds b/w O2 & H2, b-pleated- H bonds b/w regions of polypeptides e.g. spiderweb Tertiary- H-bonds, ionic bonds, disulfide bonds Quaternary- 2 alpha chains + 2 beta chains e.g Hemoglobin

Denaturation of proteins Changes in pH, salt concentration or temp. can change the shape of a protein=denature Disrupts H-bonds, Ionic Bonds, & Disulfide bridges Cant be reversed & loss of normal function

Chaperones- helps the proteins fold more efficiently(diseases from misfolding, Alzheimers disease) Protein Functions Structure/support- collagen (skin) & keratin (hair &nails) Enzymes- regulate chemical reactions Transport- hemoglobin (carriesO2 in blood) Defense- antibodies Hormones- insulin regulates blood glucose Motion- actin & myosin make up muscles

Nucleic Acids Transmits hereditary info & determines what type of proteins a cell makes DNA- composed hereditary material of the cell (genes), instructions for making proteins & RNA, AGCT, double stranded RNA- used in processes that link amino acids to form polypeptides, Ribozymes act as catalyst, AGCU, single stranded

Nitrogenous bases Purines- adenine, guanine Pyrimidines-Cytosine, Thymine, Uracil

Nucleotides Nuleic acids are polymers of nucleotides Nucleotides are made up of 3 parts, o A five carbon sugar, deoxyribose in DNA or ribose in RNA o One or more phosphate groups (make the molecule acidic) o A nitrogenous base ( nitrogen containing ring compound

Nucleotides and energy ATP-primary energy molecule in all cells GTP-transfers energy by transferring a phosphate group 1 glucose=36 ATP Chapter 4 Nucleus- Nuclear membrane + Nuclear pores, nucleolis, nucleoplasm, chromatin Mitochondria- 2 membranes, inner membrane has cristae, own maternal DNA, ATP by cellular resp. SER(no ribosomes)- lipids- detox- carbs liver E.R. RER(ribosomes)-proteins Golgi- Stack of pancakes-sorts and packages stuff from RER, has a Cisface and Transface Free in cytoplasm Ribosomes Bound to RER, Makes proteins, 2 subunits come together when making proteins Lysosomes-30-50 types enzymes, autophagy: kills itself due to illness, Aptosis: programmed death

Chapter 7

Matter- anything that has mass and takes up space Energy- Capacity to do work (change in state or motion of matter) Kilojoules (KJ)-Units of work Kilocalories (Kcal)- units of heat 1 Kcal = 4.184 KJ (memorize)

Types of energy Potential energy- stored energy, the capacity to do work Kinetic energy- energy of motion used Chemical Energy- potential energy stored in chemical bonds

Thermodynamics The study of energy and its transformations, governs all activities in the universe Open systems- exchange energy with surroundings, biological systems Closed systems- does not exchange energy with surroundings

Laws of thermodynamics 1) Energy cant be created nor destroyed, but can be converted to one form to another 2) When energy is converted from one form to another some of the energy is lost as heat Heat- kinetic energy of randomly moving particles Entropy- measure of disorder, or randomness of energy o Organized- useable energy has low entropy o Disorganized- heat has high levels of entropy o No energy is ever 100% efficient because energy is dispersed as heat, increasing entropy.

Metabolism All chemical reactions taking place in an organism

2 types of metabolism Anabolism: pathways in which complex molecules are synthesized from simpler substances (requires energy) Catabolism: pathways in which larger molecules are broken down into smaller ones (releases energy

Enthalpy (H)- total potential energy of a system Free energy (G)- amount of energy available to do work Temperature (T) H= G+TS as entropy increases the amount of free energy decreases Exergonic and Endergonic reactions Exergonic-releases energy, spontaneous downhill reaction

Endergonic- Gains free energy

Energy is required to initiate every reaction even spontaneous reactions.