final test
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| amines | Ammonia (NH3) derivatives in which one or more hydrogen atoms is replaced with alkyl or aromatic groups
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| Methylamine - how does it differ from ammonia? | a methyl (CH3) group replaces one of the hydrogen groups NH2CH3
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| amides | A derivative of carboxylic acids - an amino group replaced the hydroxyl group
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| Amides hide in Ohio | Amides take an -OH group off & add an -NH2 group
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| What is lost when amides hide in OHIO? | One hydrogren atom
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| Name an aromatic amide | Benzene can form an amide called benzamide
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| Amides - name three | UREA - phenobarbital (a barbiturate acid - sedative) - acetaminophen -
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| Name a heterocyclic alkaloids (an amine in plants) | Morphine - naturally occuring found in poppy plants
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| Give an example of an amine | Histamine -
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| Amino acids ALL love water--true or false? | FALSE - some are hydrophobic - NONPOLAR amino acids can't form bonds, are hydrophobic
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| Acidic amino acids have side chains that have a | amino group that can ionize as a weak base
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| Basic amino acids have side chains | containing a weak base that can ionize
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| Fischer projections for proteins are different because | "L" only occur in proteins
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| zwitterion has two twitter ions that fritter ions away | Zwitterions are dipolar--with a net charge of zero
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| Why is the charge important in amino acids? | Can use electrophoresis to identify sickle cell trait in newborns
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| What is a PEPTIDE? | The molecule formed when two amino acids are joined
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| What is the peptide bond? | An amide bond that forms when zwitterions react
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| fischer projections-are amino acids chiral? | Yes, but only the L are used in proteins
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| Where are peptide bonds HYDROLZED?? (it only makes sense) | in the stomach--peptide bonds are hydrolyzed (water added) in the presence of an enzyme to break down the primary structure & enable the body to digest
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| what are enzymes? | Globular Proteins that catalyze biological reactions
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| Denaturation of proteins | Occurs when there is a disruption of secondary, tertiary or quaternary bonds - but NOT the primary structure (because covalent amide bonds are not affected)
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| What denatures proteins?(5) | Heat, acids & bases, organic compounds like isopropyl alcohol, heavy metal ions like AG+, and agitation
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| How much heat to denature proteins? | Few remain active above 50degrees centigrade
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| How many amino acids provide the building blocks of proteing? | 20 amino acids
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| What is the CENTRAL element in each amino acid? | A carbon is CENTRAL to the amino group - with the amino, carboxylic acid, R group and an H atom surrounding it
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| What gives the property of being polar or nonpolar? | The R group
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| What is the normal "acid-base" state of amino acids? | Usually, they are zwitterions - meaning that they are neutral at the isoelectric point
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| How do peptides form? | when an amide bond links the carboxyl group of one amino acid and the amino group of a second amino acid
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| What is a long chain of amino acids? | a PROTEIN
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| What is the primary structure of a protein? | the SEQUENCE of amino acids
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| What forms the secondary structure? | Hydrogen bonds between peptide groups produce characteristic shapes (such as silk with its straight hydrogen bonds)
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| In globular proteins, what goes to the inside? | the HYDROPHOBIC R groups go inside
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| Alpha helix | Hydrogen bonds form a telephone cord
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| alpha-keratins | fibrous proteins that form hair, nails & skin
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| what is the most abundant form of protein in the body? | collagen - fibrils of triple helixes
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| Oligopeptides | between 2 and 10 sugars
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| ESSENTIAL amino acids | Amino acids that must be supplied by the diet because they are not found in the body
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| enzyme substrate complex | the combination of enzyme & substrate "makes it happen" the reaction is performed & product is made
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| active site | Enzymes are large, but the active site is a small region - like a pocket-that fits the structure of the substrate
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| Ex. of enzyme substrate complex | sucrose (a complex sugar) is hydrolized by sucrase (the enzyme) - creating glucose & fructose
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| Lock-and-key model | in the theory, the active site has a rigid shape which only fits the substrate
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| substrate | the molecule that reacts in the active site in an enzyme-catalyzed reaction
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| Induced-fit model | the active site on the enzyme is flexible & will fit appropriate substrates like a ship docking at a particular dock
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| What factors affect enzyme activity? | Temperature, pH, the amount of enzyme & substrate available to react (concentration)
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| What is optimal temp for enzyme activity in the body/ | 37degrees C--anything higher than 50 degrees centigrade destroys them
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| ph-what is normal? | in most cells, 7.4 is normal--some stomach cells have an acidic pH
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| does increasing enzyme concentration increase reactions? | Yes, until the enzyme molecules are saturated with substrate
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| Irreversible inhibition | Usually, toxic substances that destroy enzymes, such as insecticides
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| Irreversible inhibition - antibiotics | ex-penicillin inhibits an enzyme needed for formation of cell walls in bacteria, but not in humans
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| Classification of enzymes by function | Oxidoreductases - transferases - hydrolases - lyases - isomerases - ligases
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| Oxidoreductases | Oxidation-reduction reactions - remove 2H to form double bonds
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| transferases | transfer amino group - transfer phosphate groups
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| hydrolases | hydrolysis reactions
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| lysases | remove CO2(decarboxylases) - remove H2O (dehydrases) - remove NH3 (deaminases)
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| isomerases - | rearrange atoms to form isomers -
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| ligase | bonding molecules from synthesis of ATP
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| ISOenzymes | different forms of an enzyme that catalyze the same reaction in different cells or tissues of the body
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| zymogens | zymogens or proenzymes
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| isoenzymes as diagnostic tool | "Iso" late the disease--cells die & the isoenzymes are released from the cells instead of working--so if heart muscle isoenzymes are abundant in the blood, that indicates damage to an organ
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| effective pH range of most human enzymes | 7.35-7.45
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| temp for enzyme level | remember potato-catalase worked best at room temperature
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| Noncompetitive inhibitior | ex aspirin - binds to the cyclo oxygenase so pain-producing prostoglandins are not produced
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| Why are zymogens different? | because they are first inactive, then stored, then transported to where needed
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| ex. zymogen | insulin - first it is PROINSULIn - then a
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| another ex. zymogen | stomach acids - would eat up pancreas
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| allosteric enzymes | Enzyme that regulates the rate of reaction when a regulator molecule attaches to a site other than the active site
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| pancreatitis | a disease that results when stomach acids are not in the zymogen form, but become acid & actually eat up the proteins that make up the pancreas
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| allosteric enzyme | allo"stear"ic - stears that rate of reaction
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| feedback control | Inhibits the first enzyme from making more product when the cell has enough-will turn off until cell needs it again
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| Coenzyme | small organic molecule needed to complete a reaction
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| cofactors | metal ion needed to complete an enzyme reaction
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| metal ion cofactor-example | Iron - Fe2+ in the blood
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| vitamins | (blank)
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| what is the cofactor's principle job? | to prepare the site for enzyme activity
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| fat-soluble vitamins | A, D, E, & K
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| What vitamin do Inuits get too much of from seal liver? | A - remember "seal" A - E then D & K
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| Thiamin b1 | liver, yeast,
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| vitamins are co-enzymes | associate when needed; then dissassociate
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| ascorbic acid (vitamin C) is needed to make what? | collagen
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| Vitamin D is needed for | regulation of absorption of phosphorus & calcium during bone growth (prevent rickets)
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| Vitamin A (retinol) | eyes - sources are yellow and green fruits & vegetables
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| Vitamin E (tocopheral) | antioxidant-can get anemia without it
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| Vitamin K | fat soluble
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| Purine - two bases in DNA & RNA - how do you remember? | the shorter name has MORE rings
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| Pyrimidines in DNA - cytosine and thymine - how do you remember? | Shorter name - just one ring wi
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| Purines - in DNA & RNA | Purine - a "DAG" chow - DNA & RNA contain Adenine & guanine
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| RNA contains what base different from DNA? | uracil - remember "UR" RNA
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| RNA and DNA have RIBOSE which is what kind of sugar? | PENTOSE (five) sugar ring
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| What is the difference between DNA & RNA? | DNA is de-oxy-ribose - missing Oxygen atom on carbon '2
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| ATP adenosine 5'-triphosphate | Major source of energy
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| Phosphodiester bonds-what are they? | Phosphorus would die for ester's bondage - the phosphorus-sugar bonds which form the "ladder" section of DNA
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| complementary base pairs on DNA-why? | Remember purine & pyramidine? the width of all the base pairs is the same because they have one of each
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| complementary base pairing plays a crucial role in cell replication-true or false | TRUE
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| Remember "the last shall be first" DNA base pairs | A (adenine) with T (Thymine)
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| DNA base pairs - the other base pair | Guanine (G) and Cytosine (C) the "close" pair
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| replication forks | the open sections where DNA polymerase begins the replication process
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| replication | process of duplicating DNA by pairing the bases on each parent strand with their complementary base
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| Okazaki fragments | in "Laggin strand" short sections are synthesized
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| RNA transcription | messenger RNA is a copy of the DNA
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| RNA translation | RNA convert the information into amino acids, which are placed in the proper sequence to make a particular protein
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| Genetic code | "triplet" along mRNA - these are called codons
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| Codons - do they go on forever? | No-there are start & stop signals at the "end" of a polypeptide chain
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| What starts protein synthesis? | messenger RNA attaches to a ribosome (Large blobby thing behind strand)
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| translocation-ribosomes/tRNA | the transfer RNA detaches from the large blobby ribosome & goes to next codon group
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| Mutations-wrong instructions -two types | Substitution & frame shift
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| substitution mutation | a wrong amino acid is placed-there is a shift in the codon in mRNA
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| Mutation: frame shift | extra base - shifts everything over-all codons are incorrect due to base change
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| recombinant DNA | make insulin-DNA spliced from organisms to make new DNA
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| Ex. recombinant DNA | INsulin - human insulin is combined with bacterium to produce millions of copies of itself
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| DNA fingerprinting | a DNA sample is cut, radioactive isotope is applied, fragmenst produce "fingerprint" unique
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| viruses- | small particles which require a host cell to replicate
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| retrovirus | uses "reverse" transcription - produces a viral version of dna using the cell's DNA, then continues to reproduce
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| AIDS is retrovirus | blocked from reproducing
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| anabolic reactions | "build" large molecules like athletes build muscles
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| catabolic reactions | "jump" like cats to produce energy
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| ATP is composed of | nitrogen base adenine - ribose suger - and "TP" tri-phosphate
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| Stages of metabolism | Digestion - degradation - oxidation
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| mitochondria | enzymes catalyze the oxidation of carbohydrates, fats & amino acids
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| ATP is the bodies energy source | is obtained from the oxidation of food in the mitochondria
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| Hydrolysis of ATP releases (same as pH) | 7.3 kilojoules
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| ATP provides energy for muscle contraction | also need calcium
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| glycolysis - (wormy digestion) | glycolysis-glucose broken down to pyruvate--in the cell
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| pyruvate--needed for further reactions? | Yes-glycolysis uses energy to make energy
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| Pyruvate is used in aerobic AND anaerobic conditions--correct? | Yes, if oxygen is present
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| when is pyruvate anaerobic? | During strenuous exercise, oxygen in muscles is depleted
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| Fermentation & pyruvate | occurs in anaerobic microorganisms such as yeast
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| glycogenesis - making glycogen | Stores glucose - operate when needed
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