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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