Bio 1 Exam 1 Study Guide
Bio 1 Exam 1 Study Guide BSC2010
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This 5 page Study Guide was uploaded by clb13m on Friday January 8, 2016. The Study Guide belongs to BSC2010 at Florida State University taught by Dr. Steven Marks in Fall 2015. Since its upload, it has received 37 views. For similar materials see Biological Science 1 in Biological Sciences at Florida State University.
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Date Created: 01/08/16
Exam 1 Material Know the number of bonds that can be formed by hydrogen, carbon, oxygen, nitrogen, and phosphorus o H – 1 o C 4 o O 2 o N 2 o P – 5 Understand the differences between covalent (polar and nonpolar), ionic, hydrogen bonds, and Van der Waals interactions, and know which bonds are strongest and which are weakest. o Covalent – pairing of atoms in a chemical bond where the atoms share an electron Nonpolar – equal sharing of the electron Polar – uneven sharing of the electron o Ionic – electrical attraction between two atoms, one that has gained an electron and one that has lost one o Hydrogen bonds – electrical attraction between compounds held together by polar covalent bonds o Van der Waals Interactions – weak attraction of uncharged atoms o Strength: covalent > ionic > hydrogen bonding > Van der Waals Know that OH and NH and C=O covalent bonds are polar with the oxygen and nitrogen holding a partial negative charge and the hydrogen or carbon having a partial positive charge. CC and CH covalent bonds are nonpolar. Understand the concepts: molecular weight, mole, molarity, and be able to calculate how many grams of a substance should be dissolved in a given volume of water to make a solution of a certain molarity. o Molecular weight – sum of the atomic weights of atoms in a molecule o Mole – amount of a compound equal to its molecular weight in grams o Molarity (M) – measure of the moles of a solute dissolved in a liter of a solution Know and understand the terms hydrophobic and hydrophilic, be able to predict whether a molecule is hydrophilic or hydrophobic based on its molecular structure. Know what an acid and a base is, and understand the concepts of pH and pH scale, be able to convert pH values into hydrogen ion concentrations. o Hydrophilic – water loving; substances dissolve readily in water Molecules that have polar covalent or ionic bonds tend to be hydrophilic o Hydrophobic – substances that do not dissolve in water Molecules that are nonpolar covalent bonds tend to be hydrophobic o Acid – any substance that will dissolve in water yielding H+ and an anion – or any substance that can donate protons o Base – a substance that dissolves and produces a hydroxyl ion – or any substance that can accept protons Strong acids and bases completely dissociate in water Weak acids and bases do not completely dissociate o pH – measure of the concentration of dissolved H+ o pH scale goes from 1 (acidic) to 14 (basic) o pH = log[H+] 10^(pH) = [H+] Know what a buffer is and understand how buffers control pH o Buffers are substances that gain or lose protons depending on pH o If pH increases (becomes more basic) then the buffer will lose protons to make the solution more acidic = control the pH o If pH decreases (becomes more acidic) then the buffer will lose protons to make the solution more basic = control the pH Know the structure and general chemical activities of the major reactive groups on organic molecules, OH (hydroxyl, basic, hydrogen bonding), CO & CHO (carbonyl, hydrogen bonding), NH2 (amine, basic, hydrogen bonding), COOH (carboxyl, acidic) P04 (phosphate, charged and high energy bonds), SH (sulfhydryl, reactive, important in protein structure), CH3 (methyl, non reactive and nonpolar) o Hydroxyl (–OH) – alcohol; polar o Carbonyl (C=O)/(HC=O) – ketone if the carbonyl group is within a carbon skeleton/aldehyde if the carbonyl group is at the end of the carbon skeleton o Carboxyl (O=COH) – has acidic properties because the covalent bond between the oxygen and hydrogen is so polar o Amino (HNH) – amines; in amino acids; acts as a base o Sulfhydryl (SH) – thiols; two sulfhydryl groups can react, forming a covalent bond. This “cross linking” helps stabilize protein structures o Phosphate (PO4) – contributes negative charge to the molecule of which it is a part (2 when at the end of a molecule, 1 when located internally in a chain of phosphates); activity of proteins is often controlled by the addition or removal of phosphate groups; bonds are high energy bonds and are often used as energy currency in cells (ATP) o Methyl (CH3) – addition of a methyl group to DNA, or to molecules bound to DNA, affects expression of genes Be able to distinguish carbohydrates (sugars), lipids, and amino acids from their structural formulas. Know what a monosaccharide, disaccharide, and polysaccharide are, that glucose is a 6 carbon monosaccharide. o Carbohydrates – sugars and the polymers of sugars source of energy and carbon Monosaccharide – single sugar molecular formulas (simplest carb) Disaccharide – double sugars (two monosaccharides) Polysaccharide – polymers composed of many sugar building blocks o Lipids o Amino Acids Know that glucose forms two important polysaccharides, starch (glycogen) and cellulose. Starch is used for energy storage and that cellulose is used in plants to build cell walls (has a structural role). o Starch – plants store stockpiles of glucose in the form of starch in chloroplasts Two forms: Amylose (linear chain of 14 glycosidic linkages) and amylopectin (branched, has additional 16 linkages) o Cellulose – major structural component of the tough wall of plant cells; cellulose is a polymer of glucose, but the glycosidic linkages differ from starch. The difference is based on two ring forms for glucose: alpha (starch) and beta (cellulose) Know the general structures of the three types of lipids (Fats, Phospholipids, and Steroids) and be able to state what their main biological functions are. o Fats – energy storage Fatty acids may be saturated (all carbons have two attached H) or unsaturated (some carboncarbon double bonds) Most animals are saturated. These fats stack together to form solids (butter). Can clog arteries and cause cardiovascular disease Unsaturated fats are prevalent in plants and fish. The inflexibility of double bond prevents them from stacking. Thus they are liquid at room temperature o Phospholipids – building membranes Two fatty acids and a phosphate group are attached to glycerol; the fatty acid tails are hydrophobic, but the phosphate group forms a hydrophilic head o Steriods – are signaling molecules (hormones) They’re lipids characterized by a carbon skeleton consisting of four fused rings Cholesterol, implicated in cardiovascular disease; it’s a component in animal cell membranes and is the precursor to several steroid hormones Know that proteins are polymers of amino acids held together by peptide bonds, that each kind of protein has a unique amino acid composition (different order in which the amino acids are strung together), that cells contain thousands of different kinds of proteins and that each protein has a specific cellular function. o The different R groups have different sizes, shapes, and chemical properties o Major groups are nonpolar, polar, and charged o Its this variety in the R groups that give proteins their diverse functions Be able to draw the general structure of an amino acid, know that there are 20 different amino acids used to make proteins, and know the four different categories of amino acids based on the chemical character of their R groups (side groups) nonpolar, polar but uncharged, charged (acidic or basic). o Four different categories: Nonpolar, polar, polar Acidic (charged), polar basic (charged) o Amino Acids are joined by peptide bonds A linear chain of amino acids is a polypeptide, which have amino and carboxyl ends Functional proteins consist of one or more polypeptides Know what the 4 levels of protein structure are (primary through quaternary). Know that the tertiary structure of a protein is stabilized by interactions between amino acid R groups within a polypeptide, that these interactions are hydrogen bonding between polar but uncharged R groups, ionic bonds between charged amino acids, covalent disulfide bonds pairs of cysteins, and hydrophobic interactions (Van der Waals interactions) between amino acids with nonpolar R groups. o Primary – sequence of amino acids in the chain o Secondary – regular, repeating hydrogen bondig between the N and O components of peptide bonds In A helix, H bonding causes coiling In B pleated sheets, H bonding causes kinks o Tertiary – creates overall 3D shape, resulting from interactions between R groups o Quaternary – overall structure when two or more polypeptides interact to form the active protein; interaction between polypeptides are the same as those involved in tertiary interactions Understand what "denaturation" and renaturation of a protein means; that heat or high or low pH can cause proteins to denature, and that denatured proteins are inactive (lose their function). o Denaturation – loss of 3D structure; does not function Caused by high heat, high or low pH, anything that disrupts interactions that hold structure together o Renaturation – functional proteins, although not all proteins an renature once they are denature Were denatured, then the 3D structure was rediscovered Know the general structure and function are of the following cellular structures and organelles: plasma membrane, nucleus, ribosomes, ER (rough and smooth), Golgi, lysosomes, mitochondria, and chloroplasts. Be able to identify each of these organelles in photographs or drawings of cells. o Plasma membrane is a biological membrane that separates the interior of all cells from the outside environment. The cell membrane is selectively permeable to ions and organic molecules and controls the movement of substances in and out of cells. o Nucleus double membrane; prorated by nuclear pores; ribosomes & mRNA made in nucleolus o Ribosomes synthesize proteins (free or bound); get transported to other parts of the cell by transport vesicles o Rough ER ribosomes in RER make membrane proteins and proteins to be secreted; these proteins are transported to other parts of cell by transport vesicles; membrane factory for cell o Smooth ER synthesis of lipids; storage of calcium o Golgi sorts and moves membranes and proteins made in ER; vesicle merges and dumps sack from the ER to the golgi. The stuff in the sack gets sorted/relocated to its correct place o Lysosomes contain enzymes that help digest food or defective macromolecules or organelles to recycle their components Phagocytosis – lysosome digests food in the food vacuole that was taken into the cell Autophagy picks up organelles thats dying o Mitchondria membrane bound organelle; have own DNA/ribosomes for making its own proteins; transforms energy from one form to another; used for cellular respiration o Chloroplasts membrane bound organelle; have own DNA/ribosomes for making its own proteins; transforms energy from one form to another; used for photosynthesis Understand that the pathway for the flow of materials to the cell surface is from ER to the Golgi, to Golgi vesicles, to the plasma membrane o Vesicle goes from rough ER to cis Golgi, gets transported to transexual golgi, then is determined whether it gets transported to the lysosome, plasma membrane, or wherever the protein inside the vesicle tells it to go (mRNA) Know the major structural differences between animal and plant cells. o Plant cells have central vacuoles (bag of salty fluid that increases size of cell) with minimal cytosol increase, thylakoids (in the chloroplast), chloroplasts, and cell walls. Animal cells doesn’t have any of that. Know what the differences in cell structure are between prokaryotic cells and eukaryotic cells o Bacteria are prokaryotes. Animals, fungi, protists, and plants are eukaryotes. o Similarities: Selectively permeable plasma membrane; cytoplasm (semifluid mixture of water and organic and inorganic compounds); chromosomes (carry genes; made of DNA and protein); ribosomes (make proteins) o Differences: Eukaryotes have internal, membrane bound organelles – particularly a nucleus, prokaryotes do not
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