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biochem
final test
| Question | Answer |
|---|---|
| amines | Ammonia (NH3) derivatives in which one or more hydrogen atoms is replaced with alkyl or aromatic groups |
| Methylamine - how does it differ from ammonia? | a methyl (CH3) group replaces one of the hydrogen groups NH2CH3 |
| amides | A derivative of carboxylic acids - an amino group replaced the hydroxyl group |
| Amides hide in Ohio | Amides take an -OH group off & add an -NH2 group |
| What is lost when amides hide in OHIO? | One hydrogren atom |
| Name an aromatic amide | Benzene can form an amide called benzamide |
| Amides - name three | UREA - phenobarbital (a barbiturate acid - sedative) - acetaminophen - |
| Name a heterocyclic alkaloids (an amine in plants) | Morphine - naturally occuring found in poppy plants |
| Give an example of an amine | Histamine - |
| Amino acids ALL love water--true or false? | FALSE - some are hydrophobic - NONPOLAR amino acids can't form bonds, are hydrophobic |
| Acidic amino acids have side chains that have a | amino group that can ionize as a weak base |
| Basic amino acids have side chains | containing a weak base that can ionize |
| Fischer projections for proteins are different because | "L" only occur in proteins |
| zwitterion has two twitter ions that fritter ions away | Zwitterions are dipolar--with a net charge of zero |
| Why is the charge important in amino acids? | Can use electrophoresis to identify sickle cell trait in newborns |
| What is a PEPTIDE? | The molecule formed when two amino acids are joined |
| What is the peptide bond? | An amide bond that forms when zwitterions react |
| fischer projections-are amino acids chiral? | Yes, but only the L are used in proteins |
| 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 |
| what are enzymes? | Globular Proteins that catalyze biological reactions |
| 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) |
| What denatures proteins?(5) | Heat, acids & bases, organic compounds like isopropyl alcohol, heavy metal ions like AG+, and agitation |
| How much heat to denature proteins? | Few remain active above 50degrees centigrade |
| How many amino acids provide the building blocks of proteing? | 20 amino acids |
| 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 |
| What gives the property of being polar or nonpolar? | The R group |
| What is the normal "acid-base" state of amino acids? | Usually, they are zwitterions - meaning that they are neutral at the isoelectric point |
| 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 |
| What is a long chain of amino acids? | a PROTEIN |
| What is the primary structure of a protein? | the SEQUENCE of amino acids |
| What forms the secondary structure? | Hydrogen bonds between peptide groups produce characteristic shapes (such as silk with its straight hydrogen bonds) |
| In globular proteins, what goes to the inside? | the HYDROPHOBIC R groups go inside |
| Alpha helix | Hydrogen bonds form a telephone cord |
| alpha-keratins | fibrous proteins that form hair, nails & skin |
| what is the most abundant form of protein in the body? | collagen - fibrils of triple helixes |
| Oligopeptides | between 2 and 10 sugars |
| ESSENTIAL amino acids | Amino acids that must be supplied by the diet because they are not found in the body |
| enzyme substrate complex | the combination of enzyme & substrate "makes it happen" the reaction is performed & product is made |
| active site | Enzymes are large, but the active site is a small region - like a pocket-that fits the structure of the substrate |
| Ex. of enzyme substrate complex | sucrose (a complex sugar) is hydrolized by sucrase (the enzyme) - creating glucose & fructose |
| Lock-and-key model | in the theory, the active site has a rigid shape which only fits the substrate |
| substrate | the molecule that reacts in the active site in an enzyme-catalyzed reaction |
| Induced-fit model | the active site on the enzyme is flexible & will fit appropriate substrates like a ship docking at a particular dock |
| What factors affect enzyme activity? | Temperature, pH, the amount of enzyme & substrate available to react (concentration) |
| What is optimal temp for enzyme activity in the body/ | 37degrees C--anything higher than 50 degrees centigrade destroys them |
| ph-what is normal? | in most cells, 7.4 is normal--some stomach cells have an acidic pH |
| does increasing enzyme concentration increase reactions? | Yes, until the enzyme molecules are saturated with substrate |
| Irreversible inhibition | Usually, toxic substances that destroy enzymes, such as insecticides |
| Irreversible inhibition - antibiotics | ex-penicillin inhibits an enzyme needed for formation of cell walls in bacteria, but not in humans |
| Classification of enzymes by function | Oxidoreductases - transferases - hydrolases - lyases - isomerases - ligases |
| Oxidoreductases | Oxidation-reduction reactions - remove 2H to form double bonds |
| transferases | transfer amino group - transfer phosphate groups |
| hydrolases | hydrolysis reactions |
| lysases | remove CO2(decarboxylases) - remove H2O (dehydrases) - remove NH3 (deaminases) |
| isomerases - | rearrange atoms to form isomers - |
| ligase | bonding molecules from synthesis of ATP |
| ISOenzymes | different forms of an enzyme that catalyze the same reaction in different cells or tissues of the body |
| zymogens | zymogens or proenzymes |
| 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 |
| effective pH range of most human enzymes | 7.35-7.45 |
| temp for enzyme level | remember potato-catalase worked best at room temperature |
| Noncompetitive inhibitior | ex aspirin - binds to the cyclo oxygenase so pain-producing prostoglandins are not produced |
| Why are zymogens different? | because they are first inactive, then stored, then transported to where needed |
| ex. zymogen | insulin - first it is PROINSULIn - then a |
| another ex. zymogen | stomach acids - would eat up pancreas |
| allosteric enzymes | Enzyme that regulates the rate of reaction when a regulator molecule attaches to a site other than the active site |
| 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 |
| allosteric enzyme | allo"stear"ic - stears that rate of reaction |
| feedback control | Inhibits the first enzyme from making more product when the cell has enough-will turn off until cell needs it again |
| Coenzyme | small organic molecule needed to complete a reaction |
| cofactors | metal ion needed to complete an enzyme reaction |
| metal ion cofactor-example | Iron - Fe2+ in the blood |
| vitamins | (blank) |
| what is the cofactor's principle job? | to prepare the site for enzyme activity |
| fat-soluble vitamins | A, D, E, & K |
| What vitamin do Inuits get too much of from seal liver? | A - remember "seal" A - E then D & K |
| Thiamin b1 | liver, yeast, |
| vitamins are co-enzymes | associate when needed; then dissassociate |
| ascorbic acid (vitamin C) is needed to make what? | collagen |
| Vitamin D is needed for | regulation of absorption of phosphorus & calcium during bone growth (prevent rickets) |
| Vitamin A (retinol) | eyes - sources are yellow and green fruits & vegetables |
| Vitamin E (tocopheral) | antioxidant-can get anemia without it |
| Vitamin K | fat soluble |
| Purine - two bases in DNA & RNA - how do you remember? | the shorter name has MORE rings |
| Pyrimidines in DNA - cytosine and thymine - how do you remember? | Shorter name - just one ring wi |
| Purines - in DNA & RNA | Purine - a "DAG" chow - DNA & RNA contain Adenine & guanine |
| RNA contains what base different from DNA? | uracil - remember "UR" RNA |
| RNA and DNA have RIBOSE which is what kind of sugar? | PENTOSE (five) sugar ring |
| What is the difference between DNA & RNA? | DNA is de-oxy-ribose - missing Oxygen atom on carbon '2 |
| ATP adenosine 5'-triphosphate | Major source of energy |
| Phosphodiester bonds-what are they? | Phosphorus would die for ester's bondage - the phosphorus-sugar bonds which form the "ladder" section of DNA |
| 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 |
| complementary base pairing plays a crucial role in cell replication-true or false | TRUE |
| Remember "the last shall be first" DNA base pairs | A (adenine) with T (Thymine) |
| DNA base pairs - the other base pair | Guanine (G) and Cytosine (C) the "close" pair |
| replication forks | the open sections where DNA polymerase begins the replication process |
| replication | process of duplicating DNA by pairing the bases on each parent strand with their complementary base |
| Okazaki fragments | in "Laggin strand" short sections are synthesized |
| RNA transcription | messenger RNA is a copy of the DNA |
| RNA translation | RNA convert the information into amino acids, which are placed in the proper sequence to make a particular protein |
| Genetic code | "triplet" along mRNA - these are called codons |
| Codons - do they go on forever? | No-there are start & stop signals at the "end" of a polypeptide chain |
| What starts protein synthesis? | messenger RNA attaches to a ribosome (Large blobby thing behind strand) |
| translocation-ribosomes/tRNA | the transfer RNA detaches from the large blobby ribosome & goes to next codon group |
| Mutations-wrong instructions -two types | Substitution & frame shift |
| substitution mutation | a wrong amino acid is placed-there is a shift in the codon in mRNA |
| Mutation: frame shift | extra base - shifts everything over-all codons are incorrect due to base change |
| recombinant DNA | make insulin-DNA spliced from organisms to make new DNA |
| Ex. recombinant DNA | INsulin - human insulin is combined with bacterium to produce millions of copies of itself |
| DNA fingerprinting | a DNA sample is cut, radioactive isotope is applied, fragmenst produce "fingerprint" unique |
| viruses- | small particles which require a host cell to replicate |
| retrovirus | uses "reverse" transcription - produces a viral version of dna using the cell's DNA, then continues to reproduce |
| AIDS is retrovirus | blocked from reproducing |
| anabolic reactions | "build" large molecules like athletes build muscles |
| catabolic reactions | "jump" like cats to produce energy |
| ATP is composed of | nitrogen base adenine - ribose suger - and "TP" tri-phosphate |
| Stages of metabolism | Digestion - degradation - oxidation |
| mitochondria | enzymes catalyze the oxidation of carbohydrates, fats & amino acids |
| ATP is the bodies energy source | is obtained from the oxidation of food in the mitochondria |
| Hydrolysis of ATP releases (same as pH) | 7.3 kilojoules |
| ATP provides energy for muscle contraction | also need calcium |
| glycolysis - (wormy digestion) | glycolysis-glucose broken down to pyruvate--in the cell |
| pyruvate--needed for further reactions? | Yes-glycolysis uses energy to make energy |
| Pyruvate is used in aerobic AND anaerobic conditions--correct? | Yes, if oxygen is present |
| when is pyruvate anaerobic? | During strenuous exercise, oxygen in muscles is depleted |
| Fermentation & pyruvate | occurs in anaerobic microorganisms such as yeast |
| glycogenesis - making glycogen | Stores glucose - operate when needed |
Created by:
walterina4327