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70 Cards in this Set
- Front
- Back
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organic chemistry |
deals with organic compounds |
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cell's components |
70-95% water, rest is carbon based compounds |
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major elements in living things |
carbon, oxygen, hydrogen, nitrogen, sulfur, phosphorus |
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organic compounds |
compounds containing carbon bonded to carbon. only formed within living things (usually contains hydrogen as well) |
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inorganic compounds |
compounds that don't contain carbon bonded to carbon. found in the non-living world |
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carbon |
- 4 valence electrons - most likely to share electrons in covalent bonds- can form 4 bonds - carbon compounds can take on different shapes- straight, branched closed rings |
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hydrocarbons |
contain only carbon and hydrogen - major component of fossil fuels - store large amounts of energy |
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isomers |
compounds that have the same molecular formula but a different structural formula |
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structural isomers |
differ in arrangement of atoms |
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geometric isomers |
same arrangement, but subtle differences in the shape |
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sterioisomers |
mirror images- one is active and the other is inactive |
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functional groups |
- groups of atoms attached to the carbon skeletons - most commonly involved in chemical reactions - each gives unique properties to the molecule (ex: estrogen and testosterone are both steroids- c skeleton of four interlocking rings that only differ in functional groups |
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polymer |
large molecule consisting of many identical or similar sub-units, strung together |
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monomer |
each individual sub unit |
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condensation/dehydration synthesis |
links monomers together by removing one water molecule for each monomer added - one molecule contributes the H, one contributes the OH-- H+OH--> H20 - requires energy |
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hydrolysis |
breaking bonds in a polymer by adding water - H from water attaches to one molecule - OH from water attaches to the adjacent molecule - releases energy |
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monosaccharides |
have formula of CH2O in multiples |
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glucose |
-monosaccharide -C6H12O6 -major nutrient for cells. during cellular respiration cells extract energy stored in glucose molecules -if these monosaccharides are not used immediately, they can larger sugars for long-term storage
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disaccharides |
double sugar, consists of 2 monosaccharides joined by a covalent bond |
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maltose |
disaccharide 2 glucoses (beer) |
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lactose |
disaccharide glucose+galactose (milk) |
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sucrose |
disaccharide glucose+fructose (table sugar) |
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polysaccharides |
macromolecules- polymers in which a few hundred to a few thousand monosaccharides are linked together |
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storage polysaccharides |
store long-term energy made up of just glucose |
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starch |
storage polysaccharide polymer of only glucose - storage unit synthesized in plants - helical shape - major source of starch- potatoes, grain |
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glycogen |
storage polysaccharide polymer of only glucose - stored in the liver and muscle cells of animals - very branched - depleted in about a day in for replenished by food |
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cellulose |
- structural polysaccharide - major component of cell wall parallel cellulose molecules are held together by hydrogen bonds- arranged in units called microfibrils eventually form super-coiled fibrils - few organisms can digest cellulose- important roughage in the human diet, it stimulates the digestive tract to secrete mucus - some bacteria and microorganims can digest it- cow has bacteria inside a pack called a rumen- attaches to the stomach (mutualistic symbiotic relationship) |
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chitin |
- structural polysaccharide - found in exoskeletons of insects and other arthropods - also found in fungi- (chitin is found in their cell wall, not cellulose) |
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lipids |
have little or no affinity to water- hydrophobic very stable structure, very nonpolar |
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triglycerides (fats) |
contains three fatty acids and one glycerol |
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--fatty acids |
long carbon skeleton at one end- head consisting of a carboxyl group attached to head is a long ydrocarbon tail-- very stable, nonpolar |
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glycerol |
attaches to the fatty acids by covalent bonds |
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saturated fats |
- no double bonds between carbon atoms composing the tail of fatty acids - as many hydrogen atoms as possible are bonded to carbon skeleton - ex: animal fats- butter, lard-- solid at room temperature because they stack together well - can contribute to atherosclerosis because deposits called plaque develop on internal lining of blood vessels, blocking blood flow |
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unsaturated fats |
- contains one or more double bond in thee tail, formed by the removal of Hydrogen atoms from the carbon skeleton - has "kink" in shape wherever the double bonds occur - prevents molecules from packing together close enough to solidify - liquid at room temperature - major function- long term energy release - gram of fat stores more than twice as much energy as a gram of polysaccharides - humans store fat in adipose cells- can swell and shrink |
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phospholipids |
have two fatty acids and a negatively charged phosphate group attached to the glycerol |
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hydrocarbon tail |
- tail of phospholipid hydrophobic |
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phosphate group |
part of phospholipid - hydrophillic |
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function of phospholipid |
major component of cell membrane - arranged in a bilayer - hydrophilic heads are on the outsides in contact with water - hydrophobic tails are inside, away from water |
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steroids |
- lipids characterized by 4 interconnected rings (cholesterol) - component of membranes of animal cells - precursor from which most other steroids are synthesized
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carotenoids |
orange-yellow pigment found in plants - plays role in photosynthesis |
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proteins |
- account for more than 50% of cells - used for structure, storage, transport, signaling, movement, defense - most structurally sophisticated-each has a unique 3-D shape |
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amino acids |
- monomers - contain both a carboxyl group and an amino group - 20 kinds of amino acids make up proteins - each amino acid has one carbon center, bonded to a hydrogen atom, a carboxyl group, an amino group, and a variable chain represented by R |
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R group (side chain) |
what makes each amino acid different-- - nonpolar side chains - polar side chains - acidic amino acid- side change negative in charge - basic amino acid- side change that is positive in charge |
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polypeptide chain |
- amino acids join one another by dehydration synthesis , forming a covalent bond called a peptide bond - polymer of many amino acids linked by peptide bonds - backbone is composed of carboxyl group and amino groups and the central carbon while the side chains stick out |
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protein conformation |
protein consists of oneor more polypeptide chain twisted, wound, and folded upon itself to form a macromolecule with a 3-D shape/conformation - protein's function depends on its conformation |
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globular proteins |
enzymes and hormones |
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fibrous proteins |
used for structure (keratin) |
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primary structure |
sequence of amino acids - even a slight change in primary structure can affect its ability to function |
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sickle cell anemia |
one amino acid is substituted for another in a single position in the primary structure of hemoglobin, preventing hemoglobin from properly carrying oxygen |
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secondary structure |
segments of polypeptide chains are repeatedly coiled or folded in patterns due to hydrogen bonds along the backbone - the weak positive charge of H attached to N has an attraction to the weak negative of O of a nearby Carboxyl group |
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alpha helix |
coiled shape ex: keratin proteins with these are more elastic because Hydrogen bonds can break and reform |
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Beta pleated sheet |
chain folds back and forth and 2 regions of the chain lie parallel to one another - found in fibrous proteins- fibroin - proteins with these are stronger |
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tertiary structure |
irregular contortions from bonding between the side chains of amino acids - due to hydrophobic interaction-- amino acids with hydrophobic side chains congregate at the core of the protein, out of contact with water - also due to hydrogen and ionic bonds between side chains
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disulfide bonds |
help reinforce the conformation- form where 2 amino acids with sulfhydryl groups bond to each other |
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quaternary structure |
2 or more polypeptide chains join together ito one functional macromolecule |
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subunit |
each polypeptide chain is called a subunit - ex: collagen- helical subunits supercoiled into a larger triple helix, giving it great strength - hemoglobin consists of 2 kinds of polypeptide chains with 2 of each |
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factors determining conformation |
1. conformations occur spontaneously as the protein is being synthesized in the cel 2. if pH, salt, temp, or other environmental aspects are changed, the protein may unravel- denature-- protein becomes inactive 3. organic solvents (ether, chloroform-- nonpolar) turn proteins inside out 4. chemicals can disrupt bonds 5. heat can disrupt conformations (ex: cooking an egg) 6. protein can sometimes reform its original shape when returned to its normal environment |
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nucleic acids |
group of organic compounds in which nucleotides are connected, forming a chain - ex: DNA RNA |
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nucleotides |
monomers that compose the polymers of nucleic acids |
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3 parts of nucleotide |
1. nitrogenous base 2. 5 carbon sugar 3. phosphate group |
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polynucleotides |
nucleic acid is a type of polymer called polynucleotide |
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phosphodiester linkages |
covalent bonds that join nucleotides between the phosphate of one nucleotide and sugar of the next nucleotide resulting in repeating sugar-phosphate, sugar-phosphate |
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DNA |
- contains deoxyribose sugar - genetic material that organisms inherit from their parents - very long, consisting of thousands of genes - sequence of the bases in DNA in code instructions for all cell activities |
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RNA |
- contains a ribose sugar - acts as a messenger by bringing the genetic information in the nucleus to the ribosome - there, proteins are formed from the instrutions coded in the RNA |
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pyrimidines |
bases consisting of a single ring (form hydrogen bonds between purines and pyrimidines) |
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purines |
bases that have a double ring (form hydrogen bonds between purines and pyrimidines) |
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the double helix |
James Watson and Francis Crick discovered the shape of the DNA molecule- the double helix- 1953 - consists of 2 polypeptide chains that spiral around an imaginary axis - phosphate and sugar are on the outside of the helix, the bonds form the rungs - 2 strands are held together by hydrogen bonds between the paired bases |
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ATP |
adenosine triphosphate - made up of sugar, base, 3 phosphate groups - can transfer a phosphate group to another molecule, thereby giving off energy |
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coenzymes |
accepts hydrogen atoms and electrons from one molecule and transfers them to different sites ex: NAD+, FAD
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chemical messengers between cells |
ex- cAMP- called a second messenger, can activate proteins within the cel - cyclic AMP- monophosphate |
