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Chapter 2 and 3

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Monosaccharides   single unit, simple sugar ex: glucose, fructose, galactose  
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Disaccharides   formed by covalent bonding of two monosaccharides ex: sucrose, lactose, maltose  
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Polysaccarides   formed by covalent bonding of several monosaccharides ex: glycogen, starch, cellulose  
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Glycogen   a polysaccharides found in animal cells  
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Starch   found in plants  
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Cellulose   found in plants, humans are unable to absorb and digest it  
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What is composed of primarily hydrogen and carbon atoms?   lipids  
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What compose triglycerides?   glycerol + 3 fatty acids  
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What are saturated fatty acids?   contain carbons linked only by single bonds  
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What are unsaturated fatty acids?   contain one or more pairs of carbon linked by double bonds  
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What are polyunsaturated fatty acids?   contain more than one double-bonded pair of carbons  
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What compose phospholipids?   1 glycerol (backbone), 2 fatty acids (tail, nonpolar & hydrophobic), & a hydrophilic polar head  
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What are the functions of phospholipids?   major compound for plasma membrane, phospholipid bilayer and micelles  
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What is amphipathic property of a compound?   polar regions face the water, non polar regions face each other  
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Steroids   sex hormones: testosterone, estradiol, and cortisol  
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What is the precursor of steroids?   cholesterol  
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What are the basic structures of an amino acid?   central carbon is bonded to an amino group, carboxyl group, hydrogen, R group  
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How does each amino acid differ?   in characteristics of the R grouop  
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4 Levels of protein   Primary-sequence of amino acids Secondary-hydrogen bonding between amino hydrogen of 1 amino acid & carboxyl oxygen of another Tertiary-formation of bends & loops in polypeptide chain Quaternary-formation of proteins w/ more than 1 polypeptide chain  
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What are the 2 most common types of protein of the second level?   Alpha helixes & Beta pleated sheets  
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What are components of a nucleotide?   phosphate group, 5-carbon carbohydrate, base-containing carbon- nitrogen ring  
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DNA   Stores genetic code, cells nucleus, double-stranded, Base: A,G,C,T  
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RNA   Needed for expression of genetic code, single-stranded, located in cell's nucleus and cytoplasm, Base: A,G,C,U  
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What is the law of complementary base pairing?   G-C A-T/U  
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Genes   portions of DNA that code for a particular protein or proteins; only one sense strand contains the actual code  
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Triplets   the three-base sequence that code for amino acid  
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Codons   transcribed mRNA codons are complementary to the code in DNA triplets  
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What is transcription?   process in which RNA is synthesized using information contained in the DNA, DNA -> RNA (mRNA, rRNA, tRNA)  
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Where does transcription occur?   occurs in the cell's nucleus  
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What would happen in the post- transcriptional processing?   1: removal if introns, sliding together of exons 2: addition of CAP to 5' end 3: adding poly A tail to 3' end  
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What is translation?   process in which polypeptides are synthesized using mRNA codons as a temple for the assembly of the correct amino acids along the sequence  
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What does the initiator codon, that originates translation, codes for?   methionine (AUG)  
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Where does translation occur?   cytoplasm  
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Condensation   joining together 2 or more smaller molecules to form a larger one, water is generated as a product  
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Hydrolysis   water reacts with molecules, causing breakage of the bonds that link a molecule together  
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Oxidation   removal of electrons (or H) from any molecules; reaction of any molecule w/ oxygen  
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Reduction   addition of electrons (or H) to a molecule  
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Phosphorylation   addition of phosphate group  
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Dephosphorylation   removal of a phosphate group  
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What can affect reaction rates and how?   [E] & [S], activation energy barrier, affinity, temp., & pH  
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Enzyme   proteins that function as catalysts for reactions in biological systems  
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An enzyme doesn't affect what?   direction of a reaction, the energy released in a reaction, and the products of a reaction  
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What does an enzyme affect?   the rate of a reaction  
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What is a cofactor?   ions, metals, inorganic  
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What is the function of a cofactor?   share change for the reaction to occur, allow the substance to bind to the active site  
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What is coenzyme?   organic molecules derived from vitamins that transfer chemical groups during chemical reactions  
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What is the function of a coenzyme?   transfer small chemical groups  
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What is enzyme saturation?   the point at which, the rate of reaction reaches maximum with no further increase at a particular substrate concentration  
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Allosteric regulation   regulatory mechanism in which a modulator binds reversibly to the regulatory site on an enzyme, including a change in its conformation and activity  
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Covalent regulation   regulatory mechanism in which changes in an enzyme's activity are brought about by the covalent bonding of a specific chemical group to a site on the enzyme molecule, usually involves bonding of a phosphate group  
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Feedback Inhibition   regulatory mechanism in which an enzyme in a metabolic pathway is inhibited by an intermediate appearing downstream  
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What is the most important energy-transferring compound cells?   Adenosine triphosphate  
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Where does glycolysis take place?   cytoplasm  
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How many ATP molecules are produced (net) in glycolysis?   2 ATP molecules  
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glycolysis: the final products with available oxygen   final product of glycolysis under aerobic conditions/with available oxygen is pyruvate. 2 pyruvate Pyruvate enters the mitochondrial matrix where it is converted into acetyl CoA  
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glycolysis: the final products with limited oxygen   With limited available oxygen: Pyruvate + NADH + H+ -> lactate + NAD+ Under anaerobic conditions,pyruvate is converted to lactate in the cytosol  
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Where does the Krebs cycle take place?   mitochondrial matrix  
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Krebs cycle: its initial substrate   Acetyl CoA  
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Krebs cycle: its production (NADH, FADH2, ATP directly, CO2, H2O) in one cycle   1 ATP, 3 NADH + 3 H+, 2 CO2, 1 FADH2  
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Krebs cycle: its significant in terms of energy production.   reduces the coenzymes NAD and FAD for oxidative phosphorylation  
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Electron transport chain: location   inner mitochondrial membrane  
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Electron transport chain: hydrogen ions movement   Electrons are carried from complex I to III by coenzyme Q, from III to IV by cytochrome C. Released energy is used to transport H+ from the mitochondrial matrix to the intermembrane space against their concentration gradient  
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electron transport chain: ATP synthase   -H+ then flow in the opposite direction (down their concentration gradient) through the enzyme ATP synthase, in the process releasing energy to synthesize ATP. -NADH -> 3 ATP; FADH -> 2 ATP  
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What happens each time an electron is passed between the molecules of the electron transport chain is produced?   Energy is RELEASED each time an electron is passed between the molecules of the electron transport chain  
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What is the first electron acceptor for an NADH and a FADH?   flavine mononucleotide (FMN)is the first component of the electron transport chain that accepts electrons from an NADH molecule. FADH2 donates its electrons to coenzyme Q which at a point down stream  
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What is the final acceptor of electrons in the electron transport chain?   last electron acceptor= O2  
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Hydrogen ions activate the enzyme ATP synthase by moving from ____ to _____   down their concentration gradient through the enzyme  
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Glycogenesis   synthesis of glycogen from glucose monomers  
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Glycogenolysis   breakdown of glycogen to glucose monomers  
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Gluconeogenesis   process during which new glucose molecules can be synthesized from noncarbohydrate precursors by the liver  
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lipolysis   first stage of lipid breakdown, in regard to triglycerides, separation of the fatty acids from the glycerol backbone  
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Lipogenesis   process by which fat is synthesized from nonlipid nutrients, such as proteins and carbohydrates  
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How many ATP are generated from the complete oxidation of one glucose molecule?    
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what compound would pyruvate converted to in the low oxygen supply    
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