Survey
* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
Bio 139 Microbiology: Dr. Amy Rogers MW noon lecture Chemistry Review for 20 pt quiz on Wednesday, Sept. 13th Textbook chapter 2 Start by reading chapter summary (at the end, p. 47). You may also look at my PowerPoint for chapter 2 (this material is NOT presented in class!!!) Answer the Self Quiz questions p. 49-50; also visit textbook website for “Questions for Review”. Structure of atoms & atomic bonding: number of electrons in each shell (relationship to atomic number); predict the number of covalent bonds formed by H (1); O (2); N (3). Ions cation (+) anion (-). Define atomic weight, isotope, mole (gram molecular weight). Ionic, covalent, hydrogen bonds. Properties of each (electron loss/gain; electron sharing; polarity); how/where are they important in biological systems? What common biological molecules are held together by hydrogen bonds, which are individually weak but collectively strong? Catabolism & Anabolism: general definitions & relationship to endergonic / exergonic reactions. Water. Properties as solute; hydrogen bonding & water. Water as a reactant: dehydration synthesis & hydrolysis. Acids & Bases: pH scale (7 is neutral; higher = alkaline; lower = acidic; one pH unit change = 10X change in proton concentration). Organic molecules: Functional groups. Be able to recognize alcohol (hydroxyl), aldehyde, ketone, carboxyl (organic acid) groups. Also know amino & phosphate groups. Monomers & polymers of life. You should know what are the monomer subunits of biologically important macromolecules (carbohydrates, lipids, proteins, nucleic acids DNA & RNA). Know what types of bonds hold these monomers together in polymers, and what functional groups participate in those bonds. Carbohydrates. Monosaccharides (composed of C,H,O); glycogen, starch, cellulose as polymers of glucose; deoxyribose & ribose are components of DNA & RNA, respectively. Disaccharides: lactose. Glycosidic bonds formed by dehydration synthesis, broken by hydrolysis. Lipids. Nonpolar bonds, hydrophobic. More hydrogen, less oxygen than carbohydrates. Fats: fatty acid + glycerol head group with ester bonds (3 fatty acids, triacylglycerol; 2 fatty acids + phosphate group, phospholipid). Saturated vs unsaturated fats: presence of double bonds. Phospholipids are main component of lipid bilayers/cell membranes: hydrophilic (polar) head, hydrophobic (nonpolar) fatty tail. Steroids. Recognize general 4 ring structure. Proteins. Polymers of amino acids joined by peptide bonds between amino group of one & carboxyl group of other. What is meant by “R group”? Dehydration synthesis & hydrolysis again. Primary, secondary, tertiary, quaternary structure of a protein. What is protein denaturation? Can be caused by heat or pH change; is primarily a disruption of weak hydrogen bonds. Understand that denaturation does NOT affect primary structure. Most enzymes are proteins. What is a substrate? Nucleic acids. Subunit: nucleotide. What 3 components make a nucleotide? (base, phosphate, sugar). Backbones held together by phosphodiester bonds; double strands of DNA held together by hydrogen bonds between complementary bases (A:T, G:C). RNA: generally single-stranded; T replaced by U.