BIol 3800 1st Edition Exam # 1 Study Guide Lectures: 1 - 2Lecture 1 (August 28th- Sepetember 4th)• Difference between Prokaryotic and Eukaryotic cells-Eukaryotic cells have DNA that is enclosed within a cell nucleus where Prokaryotic cells just have their DNA floating around or in a stationary area and unprotected by a nucleus. Eukaryotic cells are more complex.Eukaryotic cells have larger and more complex ribosomes. The cytoplasm of the Prokaryotic cell has no membrane-bound organelles.• Difference between covalent bonds and noncovalent Interactions*covalent bonds- connect atoms into a molecule so within molecule*non covalent bonds- stabilize groups of atoms with and between molecules• Hydration shell (e.g when NaCl dissolved in water)water molecules that orient themselves towards the ion, they break the hydrogen bonds to theirnearest neighbors. The group of water molecules oriented around an ion is called a hydration shell.• Types of macromolecules1. Nucleic acids DNA & RNA- molecules that enable living organisms to reproduce genetic information from one generation to the next. 2. Carbohydrates-Molecules that provide fuel and build structures in the body.3. Proteins- Molecules that provide structural support, storage, transport, cell communication, movement, and defense4. Lipids-Molecules that store energy and regulate the body's metabolic processes• General structures of amino acids. how are they linked together to make a peptideAll amino acids found in proteins have this basic structure, differing only in the structure of the R-group or the side chain..The simplest, and smallest, amino acid found in proteins is glycine for which the R-group is a hydrogen (H).A peptide bonds is a covalent chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, causing the release ofa molecule of water.• How to deermine whether the amino acid is polar or nonpolar1. Non-polar: If the side chain contains a hydrocarbon alkyl group, or a benzene ring, it's going to be nonpolar. Amino acids in this group include valine, alanine, leucine, isoleucine, and phenylalanine. 2. Polar: any side chain that contains an acid, amide, alcohol, or amine will be polar. • Building block of nucleic acids, general structure of the building blockNucleic acids are polynucleotides—that is, long chainlike molecules composed of a series of nearly identical building blocks called nucleotides. Each nucleotide consists of a nitrogen-containing aromatic base attached to a pentose (five-carbon) sugar, which is in turn attached to aphosphate group.• Difference between DNA and RNADNA contains the sugar deoxyribose, while RNA contains the sugar ribose. The only difference between ribose and deoxyribose is that ribose has one more -OH group than deoxyribose, whichhas -H attached to the second (2') carbon in the ring. DNA and RNA base pairing is slightly different, since DNA uses the bases adenine, thymine, cytosine, and guanine; RNA uses adenine, uracil, cytosine, and guanine. Uracil differs from thymine in that it lacks a methyl group on its ring.• Function of polysaccharidesBasic energy sources for living organisms GLYCOGEN- an energy reserve, (stored in liver), can break down into glucose when it is needed -Precursors for other biologically important molecules---i.e. mono saccharides are used to make other molecules like glycerol and fatty acids and some amino acids. -Cellulose-structural material in plants • What is dehydration reaction?A dehydration reaction is usually defined as a chemical reaction that involves the loss of a water molecule from the reacting molecule.• Outline of a general structure and property of phospholipidThe general structure phospholipid is that it has hydrophilic (water-loving) heads and hydrophic (water-fearing) tails. Hydrophobic tails are non-polar making them insoluble in water, while the hydrophilic heads are indeed polar making them "like" water. Their functional role in cellular membranes is to control the passage of particles going through the bilayer.Lecture 2 (September 9th - September 11th) • Equilibrium and equilibrium constantThe equilibrium constant, K, expresses the relationship between products and reactants of a reaction at equilibrium with respect to a specific unit. If K > 1 then equilibrium favors productsIf K < 1 then equilibrium favors the reactants• How do enzymes catalyze the reaction, what happens to delta GEnzymes lower the activation energy for chemical reactions. Delta G remains unaffected. Enyzmes cannot affect the delta G• Different levels of protein structure1. The primary structure is the sequence of residues in the polypedptide chain.2. Secondary structure is a local regulary occuring structure in proteins and is mainly formed through hydrogen bonds between backbone atoms. So-called random coils, loops or turns don't have a stable secondary structure. There are two types of stable secondary structures: Alpha helices and beta-sheets 3. Tertiary structure describes the packing of alpha-helices, beta-sheets and random coils with respect to each other on the level of one whole polypeptide chain. 4. Quaternary structure only exists, if there is more than one polypeptide chain present in a complex protein. Then quaternary structure describes the spatial organization of the chains. • How to determine reaction rate of Km? Vmax?The quantities KM and Vmax are experimentally determined and different for each enzyme plotting the poins on the graph to determine such quantities.• What factors affect reaction rate?Factors that influence the reaction rates of chemical reactions include the concentration of reactants, temperature, the physical state of reactants and their dispersion, the solvent, and the presence of a catalyst.• Competitive and non competitive InhibitorsCompetitive inhibition is where a inhibitor has a structural similarities of a substrate. Due this the inhibitor binds to the active site of the enzyme,where normally substrate bindsNon competitive inhibition is when inhibitor possessing same structure of substrate binds to the site other than the active site of an enzyme. The substrate binds to the active site of an enzyme.• Protein folding and unfoldingProtein denaturation involves a change in the protein structure (generally an unfolding) with the loss of activity. Water is critical, not only for the correct folding of proteins but also for the