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48 Cards in this Set
- Front
- Back
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a giant molecule formed by teh joining of smaller molecules
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macromolecule
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a long molecule consisting of many similar or identical building blocks linked by covalent bonds
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polymer
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small molecules
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monomer
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monomers connecting by covalent bonds through loss of a water molecule
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condensation reaction
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molecule lost is water
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dehydration reaction
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break with water
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hydrolysis
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sugars and thier polymers
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carbohydrates
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have the genral formula CH(2)O; glucose
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monsaccharides
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two monosaccharides joined by a glycosidic linkage
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disaccharide
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covalent bond formed between two monosaccharides
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glycosidic linkage
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polymers with a few hundred to a few thousand monosaccharies
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polysaccharides
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a storage plysaccharide in plants
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strach
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a polysaccharide stored by animals
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glycogen
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polysaccharide tha make up tough cell walls in plants
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cellulose
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used by insects, spiders, crustaceans and related animals to build their exoskeletons
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chitin
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cmpounds tht have little or no affinity for water
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lipid
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two kinds of smaller molecules: glycerol adn fatty acids
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fat
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has a long carbon skeleton (16-18 carbon atoms in length)
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fatty acid
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3 fatty acids limkd to oneglycerol molecules
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triacyglycerol
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fatty acd on which all carbons in ht ehydrocarbon tail are connected by single bonds
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saturated fatty acid
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has one or more doubl bonds formed by the removal of hydrogen atoms from the carbon skeleton
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unsaturated fatty acid
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similar to fatty acids but have two faty acid tails instead of three
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phosophlipids
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lipids characterized by a carbon skeleton consiting of four fused rings
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steriods
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a steiod; is a common component of animal cell mebranes
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cholesterol
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polymers of amino acids
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polypeptides
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consists of one or morepolypeptides folded and coiled into specific confrimations
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protein
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organic molecules possessing both carboxyl and amino acid groups
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amino acid
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covalent bond between two mino acid units formed by a dehydration reaction
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peptide bond
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it is the unique sequence of amino acids in a protein
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primary structure
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coils and folds in protein structure
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secondary structure
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other main type of secndary structure in which two or more regions of the polypeptide chain lie parallel to each other
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B-pleated sheet
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consistig of irregular contorions from interactons of the various amino groups
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tetiary structure
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a type of weak chemical bond formed hen molecules that do notmix with wter coalesce to exclude the water
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hydropholic interaction
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two cysteine monomers brought together by the folding of the protein
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disuflide bridges
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overall protein structre that results from the aggregationof these polypeptide subunits
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qunternary structure
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unraveling of a protein due to pH, salt conctration, temperature or other aspect changes
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denature
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protein moelcules that assist the proper folding or other proteins
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chaperonins
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main method used to determine the exact 3 dimensional structure of a protein
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X-Ray crystallography
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a unit of inheritance
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gene
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a polymer consiting of many nucleotide monomers
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nucleic acids
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two types of nucleic acids
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deoxyribonucleic acid (DNA) and ribonucleic acid (RNA)
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nitrogenious base; has a six-membered ring of carbon and nitrogen atoms
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pyrimindine
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six-membered ring fused to a five-membered ring
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purines
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polymers of monomers
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nucleotides
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the pentose connected to the nitrogenous base
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ribose
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the pentose conected to te nitrogenous base in the nucleotides of RNA
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deoxyribose
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nucleic aid polymer
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polymucleotide
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two polynucleides that spiral around an imagenary axis
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double helix
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