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66 Cards in this Set
- Front
- Back
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Distinguish between an element and a compound.
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an element cannot be chemically broken down anymore. a compound is more than one element combined together
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Identify the 4 elements that make up 96% of living matter
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Carbon, Oxygen, Hydrogen, Nitrogen
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Describe the structure of an atom
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neutrons, protons, electrons, atomic number, atomic mass
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Define and distinguish among atomic number, mass number, atomic weight, and and valence.
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Atomic number is the number of protons. (protons=electrons) Mass number is the number of protons and neutrons.
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Given the atomic number and mass number of an atom, how do you determine the number of neutrons?
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Mass number subtract atomic number equals the number of neutrons.
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Explain why radio active isotopes are important to biologist.
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Used to sudy cell chemisty. can determine the quantity and location of radioacitvity labeled molecuels within a cellular tissue
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Distinguish among nonpolar, polar, and ionic bonds
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nonpolar-atoms in a molecuel have similar electronegativities, the electrons remain equally shared between the two nuclei. polar-one element is more electronegative, it pulls the shared electrons closer to itself. ionic- gain or lose an electron.
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Explain why weak bonds are important to libing organisms. Ex. Hydrogen bonds.
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involved in many bological signals and processes.
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Describe and compare hydrogen bonds and van der waals interactions.
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Hydrogen- can be attracted to another electronegative van der waals- all atoms and molecuels are attracted to each other.
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Explain how a molecule's shape influences its bilogical funtion.
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When atoms form covalent bonds their s and three p orbitals hybridyze to gorm four teardrop shaped orbitals in a tetrahedral arrangement.
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Write the chemical equation that summarizes the process of photosynthesis, noting the reactants and the products
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6CO_2+ 6H_2O-->C_6 H_12 O_6+ 6O_2
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Describe how the relative concentrations of reactants and products affect a chemical reaction.
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Increasing the consentrations of reactants can speed up rate of the reaction. The greater the conventration of reactant moelcules the more frequently they collide with one another and have an opportunity to react and form products.
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CHAPTER 3
Explain the relationship between the polar nature of water and it's ability to form hydrogen bonds. |
The two hydrogens on a water molecule have opposite charges. Each water molecule can then form hydrogen bonds to a maximum of four neighbors.
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List four characteristics of water that are emergent properties resulting from hydrogen
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1. organisms depend on the cohesion of water melecules 2. water moderates temperatues on Earth. 3.oceans and lakes don't freeze solid because ice floats 4.water is the solvent of life.
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Describe the biological significance of the cohesiveness of water.
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Water can move against gravitiy in plants because of this cohesion.
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Destinguish between heat and temperature.
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Heat is a measure of kenetic energy. Temperature measures the average kenetic energy of melecules in a substance.
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Explain how water's high specific heat, high heat of vaporization, and expansion upon freezing affect both aquatic and terrestrial ecosystems.
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When water freezes it expands, therefore not all of the water on eart freezes solid so the fishies live. heat of vaporization eventually turns into rain which everyone needs. water has a specific heat of 1 cal/g/*C. The amount of heat that is absorbed to change the temp.
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Distinguish among a solute, a solvent, and a solution
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Solute-substance is dissolved, Solvent-what the solute is dissolved in
Solution-2 or more substances |
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Explain how the polarity of the water molecule makes it a versatile solvent.
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The positive and negative regions of water molecules are attracted to oppositely charges ions or partially charged region of polar molecules.
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Distinguish between hydrophilic and hydrophobic
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Hydrophilic likes the water, hydrophobic doesn't like the water.
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Explain the basis for the pH scale.
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Describes how acidic or basic something is from 1-14 (1-7 acidic, 8-14 basic)
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Explain how acids and bases directly or indirectly affect the hydrogen ion concentration of a solution.
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pH declines as H+ concentration increases
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Using the bicaronate buffer system as an example, explain how buffers work.
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Substances that minimize changes in the concentrations of H+ and OH- in a solution accepting H ions from the solution when they are in excess and donating hydrogen ions to the solution when they have been depleted.
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CHAPTER 4
EXPLAIN HOW CARON'S ELECTRON CONFIGURATION DETERMINES THE KINDS AND NUMBER OF BONDS THAT CARBON WILL FORM |
has 4 valence electrons, can double bon, triple bond with itself combine with many different elements
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Describe how carbon skeletons may vary, and explain how this variation contributes to the diversity and complexity of organic molecules
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Hydrocarbons-carbon and hydrogens covalent bonding. Isomers-same moelecular formula but different structures and different properties. etc.
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Name the four functional groups and describe the chemical properties of the organic molecules in which they occur.
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Hydroxyl, Carboxyl, Amino Carbonyl (ketone and aldehyde) phosphate, methyl
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CHAPTER 5
Explainhow monomers are used to build polymers. |
Monomers are joined by removing a water molecule. (condensation reaction)
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List the four major classes of macromolecules
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Carbohydrates, Lipids, Proteins, Nucleic acids.
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Compare condensation and hydrolysis.
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condensation removes a water molecule whlie hydrolysis adds a water molecule.
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Describe the distinguishing characteristics of carbohydrates and explain how they are classified.
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Monomers called monosaccharides. cellular use for energy, energy storages, structure (C, 2H, O)_n Monosaccharides, disaccharides, and polysaccharides.
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Distinguish between monosaccharides and disaccharides.
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Monosaccharides (glucose, aldehydes and ketones, 3-7 carbons/molecule, lenear and ring forms) Dissaccharides ( 2 monosaccharides, sucrose=glucose+fructose, joined by a condensation synthesis called a glycosidic linkage).
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Identify a glycosidic linkage and describe how it is fromed.
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A dissaccharide consists of two monosaccharides joined by a glycosidic linkage, a covalent bond formed between two monosaccharides by a dehydration reaction.
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Describe the structure and funtions of polysaccharides.
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Several hundred or more monosaccharides. Energy storage: starch and glycogen. Structural: Cellulose and chitin.
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Explain what distinguishes lipids from other major classes of macromolecules.
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Diverse group (phospholipids, trigycerides, steroids, waxes) many functions are energy storage, structure, regulation, bouyancy, cushioning, insulation. C,H and O. High proportion of H.
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Distinguish between a saturated and an unsaturated fat and list some unique emergent properties that are a consequence of these structural differences.
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Saturated, at room temperature the molecules of a saturated fat are packed closely together forming a solid. Unsaturated, at room temp, the molecules of an unsaturated fat cannot pack together closely enough to form a solid. unsaturated-some double bonds.
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Describe the characteristics that distinguish proteins from the other major classes of macromolecues and explain the biologically important functions of this group.
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Monomers called amino acids, 20 different amino acids, joined by a peptide linkage, function as support, storages, transport, signaling, defense, movement, and catalyst. C,H,O,,N,S...., make up 50% of cellular dry wieght.
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Identify a peptide bond and explain how it is formed.
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after catalyzing a dehydration reaction the resulting covalend bond is called a peptide bond.
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Distinguishe between a peptide bond and a protein
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The peptide bond bonds the proteins together.
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Explain what determines protein conformation and why it is important.
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A protein consists of one or more polypeptides folded and coiled into specific conformations.
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Define primary structure
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polypeptide chain
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Describe the two types of secondary structure. Explain the role of hydrogen bonds in maintaining the structure.
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Helix or a pleated sheat.hydrogen at regular intervals along the polypeptide backbone. Only the atoms of the backbone are involved.
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Explain how weak interactions and disulfide bridges contribute to tertiary protein structure.
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consists of irregular contortions from interactions between side chains of the various amino acids.hydrophobic reaction. caused by water molecules
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Using hemoglobin as an example, describe quaternary protein structure.
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two kinds of polypeptide chains.
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Define denaturation and explain how proteins may be denatured.
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If the pH, salt concentration, temperature, or other aspects of its enviornment are altered, the protein may unrac\vel and lose it natice conformation
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Describe the characteristics that distinguish nucleic acids from the other major groups of macromolecules.
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Monomers are necleotides, condensation linkage is called posphodiester linkage, 2 types: RNA, DNA. function control heredity and control cell functions.
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Summarize the functions of nucleic acids.
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Basically tells the cells what to do
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Distinguish between a pyrimidine and a purine
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Pyrimidine have thymine, uracil and cytosine, single ring
Purines have adenine and guanine, double ring structures.. |
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Briefly describe the three dimensional structure of DNA
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Double helix
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CHAPTER 6
Explain the role of catabolic and anabolic pathways in the energy exchanges of cellular matabolism |
Catabolic pathways-glucose and other organiv fuels are broken down to carbon dioxide and water. Anabolic pathways-consume energy to build complecated molecules from simpler ones.
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Distinguish between kinetic and potential energy.
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Kinetic-energy of motion, Potential-energy the matter possesses because of its locations or structure.
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Explain in your own words the first and second laws of thermodynamics.
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Enery cannot be created nor destroyed, increase in entropy or chaos.
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Explain why highly ordered living organisms do not violate the second law of thermodynamics.
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Organisms are open systems that exchange energy and materials with their surroundings.
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Write and define eac component of the equation for free enerygy change.
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Delta G=G_final state-G_starting state.
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Describe the relationship between free energy and equilibrium.
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As a reaction proceeds toward equilibrium the free energy of the mixture of reactants and product decreases. Free energy increases when a reaction is somehow pushed away from the equilibrium.
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Distinguish between exergonic and endergonic (exothermic or endothermic)
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Exergonic releases energy and endergonic absorbs energy.
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Exlain why metabolic disequilibrium is one of the defining features of life.
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A cell can maintain desequilibrium because it is an open system. The constant flow of materials in and out of the cell keeps the metabolic pathways from ever reaching equilibrium and the cell continues to do work throughout its life.
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Describe the tree main kinds of cellular work
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1.mechanical work, such as the beating of cilia, the contraction of muscles, and the movement of chromosomes during reproduction. 2. Transport work, the pumping of substances across membranes against the direction of spontaneous movement. 3. chemical work, the pushing of endergonic reactions that would not occur spontaneously, such as the synthesis of polymers from monomers.
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Describe the function of ATP in a cell
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ATP powers cellular work by coupling exergonic reactions to endergonic reactions.
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List the three components of ATP and identify the major class of macromolecules to which ATP belongs
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nitrogenous base of adenine bonded to ribose, (RNA) and three phosphates.
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Explain how ATP performs cellular work.
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With the help of specific enzymes, the cell is able to couple the enrgy of ATP hydrolysis drirectly to endergonic processes by transferring a phosphate group from ATP to some other molecule.
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Describe the function of enzymes in biological systems.
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Enzymes speed up mtabolic reactions by lowering the activation energy.
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Explain the relationship between enzyme structure and enzyme specificity.
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each enzyme has a specific substrate it binds to.
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Explain the induced fit model of enzyme function and describe the catalytic cycle of an enzyme.
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It's like a clasping handshake. enzyme and the substrate.
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Describe several mechanisms by which enzymes lower activation energy.
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Distorting the substrate reduces the amount of thermal energy that must be asbsorbed to achieve an transition state.
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Explain how enzyme activity can be regulated or controlled by environmental factors, cofactors and enzyme inhibitors.
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pH and temperature optimum for best results, denaturation, cofactors-vitamins, Inhibitors- competative (block the active site, compete for it) noncompetative (alosteric, change shape of enzyme not competing for the active site, bind somewhere else change shap of the active site so substrate binds somewhere else.
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Explain how metabolic pathways are regulated.
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problem-enzymes work too well. Alosteric regulation, change shape of enzyme, regulate enzyme activity. feedback inhibitor end roduct acts as an inhibitor.
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