Study guide MCB 150 Compare and contrast the three domains of life Bacteria no nuclear membrane no membrane bound organelles 1 10 microns 1 chromosome circular chromosomes e coli influenza Archaea no nuclear membrane no membrane bound organelles 1 10 microns 1 chromosome circular chromosome methanogens thermophiles structurally closer to bacteria but genetically and biochemically closer to eukarya Eukarya nuclear membrane membrane bound organelles 10 100 microns more than 1 chromosome linear and in the nucleus yeast plants and animals Describe the use of sequence data to determine evolutionary relationships Carl Woese used small subunit ribosomal RNA sequences to see how closely related species were More similar closer more different farther Explain why cells remain in a narrow size range within the scale of life As the size increases the surface area to volume ratio decreases As a cell grows in size its metabolic processes increase but surface area does not keep up so not enough to import and export Large enough to sustain metabolism minimum of reactions to sustain but the bigger you get the smaller your surface area to volume ratio will be so less efficient List the functions of a plasma membrane Allows cells to maintain a constant internal environment need to sustain basic metabolism Selectively permeable barrier regulates what gets in and what gets out Is an interface for cells where information is received from adjacent cells and extracellular signals Has molecules that are responsible for binding and adhering to adjacent cells Describe the general features of a bacterial cell Usually rod shaped sometimes spherical all about same size Capsule not everyone thick mucosal layer of complex carbohydrates protection keep cell from drying out allow to stick is not necessary to survive but once removed may not be infectious Cell wall Plasma membrane Cytoplasm o Genetic material Nucleoid o Ribosomes Identify the major organelles in an animal cell and list their functions Nucleus replicate and maintain genomes distribution of genetic info assembly of ribosomal subunits Mitochondria many present ATP synthesis where cellular respiration occurs Rough endoplasmic reticulum double membrane closest to nucleus many ribosomes attached synthesize proteins proteins for secretion Smooth endoplasmic reticulum no ribosomes no active synthesis more lake tubules still connected to outer membrane of nucleus to rough er to smooth er synthesis of lipids detox calcium storage Golgi apparatus everything from RER processes and ships out sorts and distributes Ribosomes some are on rer free floating not organelle o Polyribosomes multiple ribosomes making the same copy of the same protein Compare and contrast condensation and hydrolysis reactions Condensation monomers are attached covalent bond is formed water lost reversible Hydrolysis water in monomer out this is why you need food broken down for amino acids List the features shared by all carbohydrates Polysaccharides are made from condensation reactions bringing together monosaccharaides Uses energy sources structural roles like insect exoskeletons and cell walls or cell identification and recognition General formula Cn H2O n with a backbone of H C OH Alpha C OH bond below beta C OH bond above Hexose sugar C12H22O11 List the biologically relevant monosaccharides and provide an example of each Glucose Galactose Fructose Explain the difference between aldose sugars and ketose sugars Aldose c o at the end ketose c o in the middle Describe the formation of a glycosidic linkage and classify it in the most specific terminology available Dehydration synthesis Glucose contributing carbon 1 is an alpha glucose therefore alpha 1 4 glycosidic linkage Describe the type of monomer the type of linkage the branching if any and the major functions of the following polysaccharides starch glycogen and cellulose Cellulose the most abundant carbon containing compound on earth found in plant cell walls linear unbranched polymer of glucose monomers linked by beta 1 4 glycosidic linkages linear polymers held together by hydrogen bonding with neighboring strands Starch found chiefly in seeds fruits tubers roots and stems of plants energy storage helical unbranched or loosely branched polymers of glucose monomers within chains alpha 1 4 linkage chain branch by connecting other chains with alpha 1 6 glycosidic linkage Glycogen found in muscle and liver cells of animals energy storage helical highly branched polymers of glucose same linkages as starch Provide examples of the functions of carbohydrates in cells Recognition for cells Energy storage Cell wall Describe the general structure of an amino acid Alpha carbon center of amino acid Left side amino group or N terminus Right carboxyl or c terminus Top hydrogen Bottom r group Explain the formation of a peptide linkage Condensation reaction amino group of incoming with carboxyl group of existing proteins are built in N C direction Compare and contrast the classes of amino acids and the consequence of being in a given class Uncharged but polar has an oxygen Uncharged and non polar hydrophobic carbons or hydrogen N in a ring and S equal to H Positively charged basic proton acceptor accepted Negatively charged acidic proton donator donated List the levels of protein organization and identify the stabilizing forces at each level Primary linear sequence of amino acids from N C all proteins have a unique primary structure Secondary first level of folding hydrogen bonds between peptide linkages peptide backbone is polar independent of R groups so in most proteins alpha helix and beta pleated sheets sheets arrow towards c terminus Prion misfolds spongiform encepholopathies Tertiary unique 3D folded structures final confirmation of some proteins due to interactions between R groups with each other and backbone stabilized by H bonds between polar side chains h bonds between hydrophilic side chains and a basic amino acid ionic bonding between acidic and basic amino acid hydrophobic clustering of nonpolar side chains van der waals disulfide linkage only cysteine b c its chemically available for reaction water is stabilizing force drives hydrophobic inside lines up sites for functional activity of that protein Quaternary found in proteins with multiple polypeptide chains subunits 2 identicalhomodimer 2 different heterodimer Explain the process of protein denaturation and renaturation including the use of chaperones when necessary