Bio 201 1st EditionExam # 1 Study Guide Lectures: 1 – 9 (10 is on test, but not included)Lecture 1 (1/26/15)Covalent bonds- Electrons that exist in pairs, considered stable. Unpaired electrons are not stable. Some atoms can have multiple covalent bonds. Hydrogen- 1 bond, Carbon- 4 bonds, Nitrogen- 3 bonds, Oxygen- 2 bonds, Sulfur- 2 bonds. Electronegativity- The tendency to attract electrons. Ionization Energy- Differ with different electronegativity’s. This is the minimum amount of energy required to remove an electron. Cations= positive Anions=negativeFunctional Groups- Know compound and formula of hydroxyl, carbonyl, carboxyl, amino, and sulfhydryl. Ionic Bonds- Cations and anions come together to form these. Opposites attract. When formed the pair becomes stable. Van der Waal Interactions- All nonpolar molecules only have this. These are hydrophobic or “water fearing”Lecture 2 (1/28/15)Bond Types- Covalent> Ionic> Hydrogen> Van der WaalHydrogen bonds- Polar molecules containing atoms with opposite charge. Charge Asymmetry- Dipole, covalently bonded atoms have small differences in electronegativity. pH Formula: pH= -log of concentration. For example, [H+]=10^-7 then pH=7pH Scale- <7= ACID & >7=BASE & 7=neutralBuffer- Something that has the ability to change pH when added to an acid or a base. Water is aterrible buffer.Lecture 3 (1/30/15) Biological Macromolecules: Proteins- Used for function (enzymes), signaling, and structure. Their monomer unit is amino acids. Lipids- Used for compartmentalization, energy storage, and signaling. Lipids do not form polymers. Polysaccharides/ Carbohdyrdates- Used for energy storge and structure. Their monomer is monosaccahrides. Nucleic acids- Used for energy storage and function. These are the blue print of the cell. Their monomer is nucleotides. Polymerization- The reaction that forms the monomers into polymers. This reaction is a condensation reaction because it realease water. The release of water also requires energy. This reaction decreases entrapy or disorgnization. Depolymerization- The break down of polymers. We use this hydrolisis reaction when we break down our food to get energy. This is a hydrolisis reaction because it consumes water, therefore energy is released. Amino Acids- The monomer of proteins. The structure of amino acids is a carbon in the middle attatched to a carboxylic acid (CH3) and an anime (NH3), there is also a R group or side chain which tells us which amino acid the structure will be. Amino acids are chiral meaning the molecules are asymmetric. Chiral structures can either be Left handed (Levo) or Right handed (Dextro) All amino acids are Levo besides Glycine. R Side Chain- Can be either nonpolar, polar, or a special case. 1.Nonpolar- Hydrophobic, contain all Carbons and Hydrogens.2.A. Polar uncharged- Contain –OH or both –NH2 and Carbon double bonded to OB. Polar charged- Contain –NHx or –COOH 3. Special Cases:Glycine- Not chiral, we group as nonpolar but really could be with any.Proline- Have rings which restrict flexibility of backbone. “helix-breaker”Cysteine- -SH form disulfide bonds. –S –S – Lecture 4 (2/2/15)Protein Structure Levels:Primary 1- The amino acid sequence of the protein. Contains covalent bonds.Secondary 2- Contains a-helix- which form through h-bonding between groups on thepolypeptide backbone, and B-sheets- which are intermolecular h-bonds between different polypeptide or intramolecular h-bonds between different segments of the same polypeptide. Hydrogen and Ionic bonds are needed for the function of secondary structure. When boiled the function stops, so we know the hydrogen and ionic bonds are broken, but covalent bonds are not. Tertiary 3- The 3D structure of a single polypeptide chain. Contains secondary structure and R-group. This structure is the functioning protein. Contains disulfide (covalent) bonding, ionic bonds, hydrogen bonds, and Van der Waal. Quaternary 4- Structure resulting from interaction of multiple polypeptide subunits. Contains allbonding types. Lecture 5 (2/4/15)Changing an Amino acid sequence: Can result in diseases such as sickle cell anemia. Glucose/Sugar- Contains formula Cx(H20)y. Glucose is the most important form of energy storage. A glycosidic linkage is formed when sugars polymerize. This linkage is formed by and Oxygen connected to a sugar on each side. Check lecture 5 diagram on UBlearnsGlycogen- Sugar used for energy storage, animals can digest this and there is an a-1,4 glycosidic linkage.Cellulose- Sugar used for structure, animals cannot digest this, and there is a B-1,4 glycosidic linkage. Lipids- Fatty acids, Triglycerides, Phospholipids, and Steroids. Fatty acids- Secondary energy source when metabolized, R-group is CH2. Includes trans-fats which are unsaturated bent (cis) fatty acids. Triglycerides- Derived from Fatty acid, but also have a host. Primary storage of fatty acids and energy. Phospholipids- Derived from fatty acid with 2 hosts. Contain a long water hating tail and a waterloving head. Steroids- Contain a 4 fused ring structure, and are not derived from a fatty acid.Lecture 6 (2/6/15)Nucleic Acids- Used for information storage and function of a cell. Contain phosphorous. RNA orDNA. DNA transcribes to RNA. RNA translates to DNA. This is the Central Dogma.DNA- Contains Deoxyribose sugar. Contains bases dATP, dGTP, dCTP, and dTTP. DNA has a doublehelix structure which is antiparallel. Hydrogen bonds hold DNA strands together. G-C and A-T. RNA- Contains ribose as its sugar. Have bases of ATP, GTP, CTP, and UTP. Both RNA and DNA polymerize 5’ 3’Lecture 7 (2/9/15)3 types of RNA:mRNA- messenger RNA which gets translated into protein.tRNA- transfer RNA which brings amino acids to growing polypeptides.rRNA- ribosomal RNA, makes of 50% of ribosome, catalyzes polymerization of polypeptides. Prokaryotic- Bacteria and Archaea, known as the “bad nut”, does not contain a nucleus. Eukaryotic- Contains nucleus, loss of peptidoglycan in cell wall, gain of cytoskeleton, contain membrane bound organelles, and have an increased cell size. Plants, Fungi and Protists are apart of the eukarya.Endosymbiosis:Mitochondria- Anaerobe ingests aerobic bacterium but does not digest, this bacteria divides intracellularly, therefore some traits are inherited by each daughter cell. Evolution causes the loss of essential function which leads to bacteria no longer being able to live outside of cell alone leading to