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Chem 313 Final Exam Review

by: Anna Kretschmar

Chem 313 Final Exam Review Chem 313

Anna Kretschmar
Cal Poly
Survey of Biochemistry and Biotechnology
Dr. Steve Wilkinson

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practice questions with material from the whole quarter enzymes, proteins, cellular respiration, etc. minus transcription, translation, and replication because he posted questions with answers on...
Survey of Biochemistry and Biotechnology
Dr. Steve Wilkinson
Study Guide
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This 0 page Study Guide was uploaded by Anna Kretschmar on Monday March 14, 2016. The Study Guide belongs to Chem 313 at California Polytechnic State University San Luis Obispo taught by Dr. Steve Wilkinson in Winter 2016. Since its upload, it has received 113 views. For similar materials see Survey of Biochemistry and Biotechnology in Chemistry at California Polytechnic State University San Luis Obispo.


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Date Created: 03/14/16
Chem 313 Final Exam Review 1 On a MichaelisMenton plot what happens to Vmax and Km when the concentration of enzyme is halved 2 Why does a MichaelisMenton plot plateau at higher concentrations of substrate 3 If one enzyme A has a Km of 15 M and another enzyme B has a Km of 28 M then which enzyme has a higher af nity for its substrate 4 You make a Lineweaver Burk plot with secmM vs 1mM and get the equation y042x 084 What is Vmax and what is Km 5 Which class of enzymes is the one that joins two molecules and is usually powered by ATP Which enzyme class is responsible for adding a functional group to remove a double bond or remove a functional group to form a double bond 6 What is the difference between an aldose and ketose carbohydrate 7 What determines the rate of a reaction 8 Why is the alpha helix a stable structure in the secondary structure of proteins 9 What are three things that can cause a protein to denature 10What are the eight types of noncovalent bonds in order or strongest to weakest 11What are the functional groups in this molecule aspirin 12 Why do phospholipids which have long hydrophobic chains spontaneously form membranelike structures when placed in water 13 You have a solution of HCL that has a pH of 25 What is the concentration of HCL needed to make this solution 14 What is the pH of a 0000565 M solution of NaOH 15 Why does melting point decrease as a fatty acid becomes more unsaturated 16 How is a glycolipid different from a triacylglycerol How is it different from a phospholipid 17 Compare and contrast facilitated diffusion and active transport 18 Which is a purine and which is a pyrimiche 19 What happens to pyruvate when there is not oxygen present during glycolysis What is a product and how is it useful 20 Where are each of the following processes located in the cell How much ATP is produced by each Glycolysis Bridge step Citric acid cycle 21 What is a main difference between prokaryotic cells and eukaryotic cells 22 What are the four main groups of amino acids Be able to identify examples 23 How do enzymes affect a chemical reaction Do they change any of the reagents 24 What are the different functions of carbohydrates in organisms 25 At what stages in the electron transport chain are protons pumped into the intermembrane space Why is this ow of protons important for ATP synthesis 26 ATP is the currency of the cell because it is kinetically stable What is meant by this 27 What is the difference between primary active transport and secondary active transport 28 What are the two classes of metabolism 29 What are the main classes of enzyme inhibitors and what are their de ning characteristics 30 What are the basics facts about each of the four levels of structure in proteins ANSWERSH FYI NO transcription translation DNA replication because he provided answers onine Don t forget to study that too Vmax is halved as well while Km stays the same because it is a property of the substrate The reaction reaches its equilibrium point faster because there is more substrate to bind with enzyme All the enzyme becomes saturated so the graph attens out The lower Km means a stronger af nity therefore enzyme A has a stronger af nity for its substrate Vmax 119 mMs use 1y intercept to get this Km 5 mM use slope which is KmVmax Ligase is the enzyme that joins two molecules Lyase is the enzyme that adds and removes functional groups to change double bonds An aldose has an aldehyde in the linear representation while a ketose has a ketone The activation energy The lower the activation energy the quicker the reaction will occur The helix is stabilized by hydrogen bonds between the amino group of one amino acid and the carbonyl group of another amino acid four places down the polypeptide chain Protein denaturation can occur when there is an increase in temperature a change in pH or a change in the salt concentrations in the cell Too high of temps cause the bonds to break each protein has a speci c pH it is the most ef cient at and salt concentrations can change the charge on amino acids which can change the way the protein folds 10lonic ion dipole hydrogen dipole dipole ion induced dipole dipole induced dipole London dispersion Van der Waals 11Aromatic ring double bonded ring alcohol OH carboxylic acid 0 OH 12The hydrophobic effect causes the nonpolar chains to turn towards each and clump together to form a membrane like structure 13Use pH ogH to solve and get 0032 M HCL 14Use pOH ogOH to get the pOH then use pH pOH 14 to get a pH of 975 15Unsaturation is a result of more double bonds These double bonds don t allow the fatty acid carbon chains to bend as well so they cannot stack together as tightly This loose packing is what decreases melting point 16A glycolipid has a shingoshine backbone a carbohydrate and one fatty acid A phospholipid has a phosphate group instead of the carbohydrate A triglyceride is a glycerol with three fatty acids 17Facilitated diffusion is a type of passive transport so it does not require energy but active transport does because molecules are moving against their gradient for active transport In both cases a transporter is required 18The left is a purine because it is larger The right is a pyrimidine because it is smaller 19When there is no oxygen then pyruvate is used for ethanol or lactate fermentation These processes regenerate NAD to be used in glycolysis 20Glycolysis cytoplasm 2 ATP Bridge step mitochondrial matrix 0 ATP Citric acid cycle mitochondrial matrix 2 ATP total so one per cycle 21Eukaryotic cells are highly compartmentalized and is surrounded by a double nucleus Prokaryotes are less organized 22Amino acids are classi ed as polar nonpolar negative charge and positive charge Nonpolar mainly have carbons and hydrogens in their R group and polar will have nitrogen and sul de as well The charged ones have the corresponding charges 23Enzymes only speed up the rate of the reaction by lowering the activation energy They do not change the concentrations of the products or reactants 24Carbs are good for energy storage structural roles and are components of other important biomolecules 25When NADH binds to complex I 4 protons are pumped when electrons are transferred from Q to complex Ill 4 more protons are pumped and when electrons are transferred from C to complex IV 2 more protons are pumped This is important because it creates a proton gradient that allows for ATP synthase to be powered 26ATP has a high activation energy so it is easier for the cell to control the molecule ATP won t randomly break down because so much energy is require to do so 27Primary get is energy input from chemical reaction that involved ATP hydrolysis An example is the sodium potassium ATPase ATP hydrolysis causes a conformational change in the protein that allows each of the molecules to go against its gradient Secondary gets its energy from one molecule moving with its gradient which allows the other to move against its own 28Cataboism transforms a fuel molecule into a form of useful energy Anabolism uses a precursor molecule and energy to create a more complex molecule The main difference is catabolism make energy while the other uses energy 29Competitive inhibitors resembles the substrate and bind in the active site Uncompetitive bind only to the ES complex which prevents the product from forming Noncompetitive can bind to the enzyme or ES complex but not in the active site This also prevents the product from forming 30Primary structure is the linear sequence of amino acids Secondary is the arrangement of the amino acids that are near one another usually forming alpha helices or beta sheets Tertiary is the arrangement of amino acids not near each other which is where the disul de bonds come in to help with folding Quaternary is how different polypeptide chains arrange


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