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81 Cards in this Set
- Front
- Back
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macromelecules |
-carbs -lipids -proteins -nucleic acids -thousands of covalently connected atoms |
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polymer |
-covalently linked monomers |
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monomers |
-subunits -building block molecules
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3 classes are polymers |
-carbs -protiens -nucleic acids |
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dehydration reaction |
-2 monomers covalently linked together -loss of H2O |
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hydrolysis |
-polymers go to monomers by -H2O added to break bonds |
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carbs |
-sugars and sugar polymers -monosaccharides -polysaccharides |
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polysaccharides |
polymer of monosaccharides |
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monosaccharides |
-(CH2O)x -most common is glucose C6H12O6 -classified by carbonyl group aldose or ketose -# of carbons |
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disaccharide |
-dehydration reaction joins 2 monosaccharides -covalent bond=glycosidic linkage |
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polysaccharides |
-storage and structured roles -as plants store as starch -structures and functions determined by -monomers -positions of glycosidic linkages |
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fats |
-glycerol and 3 fatty acids -glycerol = 3C Alc -hydroxil group attached to each carbon -fatty acid |
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fatty acid |
carboxyl group attached to carbon skeleton |
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fats are |
hydrophobic -water molecules form hydrogen bonds with each other and exclude fats |
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in a fat three fatty acids are joined to glycerol by an |
ester linkage creating a tryglicericle? |
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storage polysacharides |
-starch in plants -glycogen in animals |
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starch in plants |
-glucose polymers stored as granules in chloroplasts and plastids -simplest=amylose |
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glycogen in animals |
-stored mainly in the liver and muscle cells(burn sugar) |
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structured polysaccarides |
-cellulose majjor component of plant cell walls -polymer of glucose -glycosidic linkage diff -the diff is based on two ring fors for glucose: alpha and beta |
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polymers with alpha glucose are |
helical |
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polymers with beta glucose are |
straight -straight structures H atoms on 1 strand can bond with OH groups on other strands parallel celluclose molecules -grouped into microfibris -strong buildign materials for plants |
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enzymes that digest starch by |
hydrolizing alpha linkages -can't hydrolize beta linkages in cellulcose |
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cellulose in human food |
-passes thru the digestive tract as insoluble fiber -some microbes use enzymes to diges cellulose -many herbavores from cows to termites hae symbolic relationships with these microbes |
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chitin |
-a structural polysaccharide -exoskeleton of arthropods -also provides structural support for the cell wall of many fungi |
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Lipids |
-dont form polymers little or no affinity for water -hydrophobic -most of th emolecule is hydrocarbons -nonpolar covalent bonds -fats, phospholibids, stereods |
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phospholipids |
--two fatty acids and one phosphate group attached to glycerol -phosphate group and attachemnts leading to hydrophilic head |
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Phosphates in water |
-self assemble into bilayer -hydrophobic tails pointing toward middle -bilayer in cell membranes -phospholipids |
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phospholipids |
-major componenet of all cell membrands |
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steroids |
-lipids with carbon skeleton=four fused rings =-cholestoral -essential in animals -high lvels may contribute to cardiovascular disease |
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cholestoral |
-component in animal cell membranes |
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fatty acids vary |
-in length number of carbons number and location of double bonds -saturated fatty acids -unsaturated fatty acids
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saturated fatty acids |
-max number of hydrogen -no double bonds -solid at room temp most anila fats -caridovascular disease -hydrogenization |
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unsaturated fatty acids |
-1 or >1 double bonds -or oils liquid at room temp and plant and fish fats |
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hydrogenization |
-converts unsaturated to saturated |
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partially hydrogenated veg oils |
-unsaturated fats with trans double bonds |
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trans fats |
-worse than saturated fats for cardiovas disease |
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essential fatty acids |
-we can make ourselves -not synthesized in human body -mmust be supplied in diet -omega unsaturated fatty acids -req for normal growth -protection agaisnt cardiovascular disease |
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major function of fats |
-energy storage -fat store for mammals in adipose cells |
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adipose tissue also |
-cushions vital organs -insulates |
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protein function |
-50 percent of dry mass of msot cells -structural support -storage -transport -cellular com -movement -defense agaisnt foreign substance |
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enzymes |
-catalyst made of protein -speed up chemical reactions -repeatedly -carry out metobolic processes of life |
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polypeptides |
-unbranched polymers of amino acids -protient=one or more polypeptide -bio functional molecule |
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amino acid monomers |
-carboxyl and amino groups -properties due to chains= R groups |
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amino acid polymers |
-amino acids linked by peptide bonds -polypeptide -polypeptides |
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polypeptide |
-polymer of amio acids |
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polypeptides |
-a few to more than a thousand monomers |
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each polypeptide has |
-unique linear sequence of amino acids with a carboxyl end (c terminus) and an amino end ( N terminus) |
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protein structure and function |
-a functionla protein consists of oneo r more polypeptides precisely twisted, folded. and coiled into a unique shape |
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four levels of protein structure |
-the primary structure of a protein is it s unique sequence of amino acids -secondary structure found in most proteins cosits of coils and folds in the polypeptids chain due to H bonds -tertiary strucutre is determiend ggy interactions amond various side chains R groups -quaternary structure results when a protein consists of mulitple polypeptide chians |
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primary structure |
-sequence of amino acids determined by inherited genetic info |
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secondary structure |
--hydrogen bonds between repeating carbonyl and amino groups on polypeptides backbone -beta pleated sheet -alpha helix |
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tertiary structure |
-interactions between r groups 1 hydrogen bonds 2 ionic bonds 3 hydrophobic interactions 4 van der waals interactions strong covalent bonds called disulfide bridges may reinforce the proteins structure |
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quanternary structure |
-two or more polypeptide chains from 1 protein macromolecules -collagen -hemogloben |
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collagen |
-fibrous protein -three polypeptides cailed like a rope
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hemoglobin |
-globular protein -four polypeptides : two alpha and two beta chains |
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sickle cell disease: change ina primary structure |
-slight change inprimary structure -can affect a protiens structure and fucntion -sickle cell disease -inherited blood disorder |
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what determines protien structure |
-physical and chemcial affects struture -alternations in 1ph 2salt concentration 3 temp 4 envi factors -can cause roten to unravel -this loss of a proteins native structure is called denaturation -bio inactice |
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protein folding in cell |
-most proteins go thru several stages to form a stable structure -chaperonins -Diseases such as alzheimers, parkinsons, and mad cow disease are assocated with misfolded proteins |
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chaperonins |
-protein molecules -assitt proper folding of other proteins |
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nucleic acids |
-store -transmit -help express hereditary info -amino acid sequences of a polypeptides -genes are mad of DNA |
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amino acids sequences of a polypeptides |
-programmed by genes |
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Genes are made of DNA |
-nucleic acid -made of monomers called nucleotides |
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two types of nucleic acids |
-DNA-deoxyribonucleic acid -RNA- Ribonucleic acid |
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DNA |
-provides direction for its own replication -directs synthesis of messanger RNA (mRNA) and though mRNA controls protein synthesis
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protein syntheis |
occurs on ribosomes |
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nucleic acids are |
-polymers called polynucleotides |
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each polynucleotide is made of |
-monomers called nucleotides |
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each nucleotide consists of |
-nitrogen basse -pentose sugar -phosphate groups |
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the portion of a nucleotide without the phosphate group is called |
-nucleoside |
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nucleoside |
-nitrogenous base+sugar |
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the two families of nitrogenous bases |
-pyrimidines(cytosine, thymine, and uracil) -have a single 6 membered ring -Purines-(adesine and guanine) have 6 membered ring fused to a 5 membered ring |
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nucleotide |
-nucleoside+phosphate group |
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nucleotide polymers are linked together to build |
-polynucleotide |
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adj nucleotides are joined by |
-covealent bonds that form between the OH group on the 3' carbon of one nucleotide and the phosphate on th e5' carbon on the next -these links create a backbone of sugar-phosphate units with nitrogenous bases as appendages -the sequencce of bases along the DNa or mRNA polymer is unique for each gene |
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RNA molecules usually exist as |
-single polypeptide chains |
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DNA molecules havet 2 |
-polypeptides sprialling around an imaginary axis forming a double helix |
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in DNA the double helix |
-the two backbones run in opposite 5'-3' directions from each other an arragement refered to as antiparallel |
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one DNA molecules includes many |
-many genes |
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the nitrogenous bases in DNa |
-pair up and form hydrogen bonds: adenine always with thymine and guanine always with cytosine -called complementary based pairing |
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complementary based pairing |
-can also ocur between two RNA molecules -or parts of the same molecules
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in RNA thymine is replaced by |
-uracil so A and U pair |
