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biocampbell 7ed ch 5
vocab
| Question | Answer |
|---|---|
| macromolecules | a giant molecule formed by the joining of smaller molecules. ex. polysacchrides, proteins and nucleic acids |
| polymer | long molecule of similar or identical monomers |
| condensation reaction/dehydration reaction | a reaction where two molecules become covalently bonded to each other through the loss of a molecule- usually water |
| polysaccharides | polymer of many monosachharides formed by dehydration reactions |
| enzymes | specilized macromolecules that speed up chemical reactions in cells |
| monosaccharides | simple sugars/ carbs. can act alone or serve as a monomer in disacchrides and polysacchrides |
| disaccharide | double sugar, 2monosaccharides joined by a glycosidic linkage formed during dehydration synthesis |
| glycosidic linkage | covalent bond between monosaccharides by a dehydration reaction |
| glycogen | polymer of glucose that is extensively branched. stored in liver and muscle cells. hydrolysis of glycogen in these cells releases glycogen when the demand for sugar increases |
| cellulose | polysaccharide -plant cell walls |
| lipids | hydrophobic- hydrocarbon regions |
| fat/triglyceride | 3 fatty acids each joined to glycerol by a ester linkage |
| glycerol | alcohol and 3 carbons each with a hydroxyl group and a carboxyl group |
| fatty acid | long carbon skeleton- carboxylic acid |
| saturated fatty acid | a fatty acid in whichall carbons in the hydrocarbon tailare connected by single bonds-maximizing the amount of hydrogen atoms attatched to the carbon skeleton |
| unsaturated fatty acid | a fatty acid consoting of one or more double bonds between the carbons in the hydrocarbon tail. this bonding reduces the amount hydrgen atoms attached to the carbon skeleton |
| phospholipids | glycerol, two fatty acids and a phosphate group hydrophobic tails hydrophilic head- form bilayers membranes |
| steroids | lipid with a carbon skeleton of four fused rings |
| cholesterol | component of animal cell membranesprecursor from which other steroids are synthesized |
| polypeptides | polymers of amino acids |
| protein | one or more polypeptides folded or coiled into a 3-d structure |
| amino acids | organic molecules of carboxyl and amino groups |
| peptide bond | 2 amino acids with carboxyl group next to amino group (joined by dehydration) result is a peptide bond |
| disulfide bridges | covalent bond formed when the sulfur of one cysteine monomer bonds to another cysteine monomer |
| denaturation | protein unraveled- loseshape can happen with a change in shape npH or salt concentration |
| chaperonins | unfold and refold prteins-edits them |
| sickle cell disease | substitution for valine where their should be glutamic acid in the primary structure of homoglobinsickle cell crisis when the wierd shaped blood cells cause clots |
| x ray crystallography | a technique that depends on the diffraction of an x ray beam bythe individual atoms of a crystilized molecule to study the 3D structure of the molecule |
| gene | unit of inheritance,DNA is made up of genes |
| nucleic acids | DNA, RNA |
| deoxyribonucleic acid | provides direction for its replication, directs rna |
| RNA | protein synthesis(ribosomes), mRNA directs protein synthesis to direct production of polypeptides |
| polynucleotides | nucleic acids that exist as polymers. monomers are nucleotides(nitrogenous base,5carbon sugar,phosphate group) |
| pyrimidine | 6 membered ring of carbon and nitrogen atoms. Members:cytosine, thymine, uracil(RNA bonds with A) |
| purine | 5 membered ring, adenine and guanine |
| ribose | sugar connected to the nitrogenous base in RNA |
| deoxyribose(lacks oxygen on carbon) | sugar connected to the nitrogenous base in DNA |
| Protein Structure: Primary | unique amino acids and genes. long chain |
| Protein Structure: Secondary | coils and folds. Hydrogen bonds between the polypeptide backbone bones. O and N atoms of the backbone have a partially negative charge |
| helix(secondary structure) | coil held by H bonds every 4th amino acid |
| pleated sheet(secondary structure) | 2 or more regions in the polypeptide chain lying side by side are connected by H bonds between parts of the two parrallel polypeptide backbones |
| tertiary structure | shapes the protein-determined by side chains of amino acids |
| hydrphobic interaction(tertiary stucture) | polypeptide folds, hydrphobic(nonpolar) side chains clusterin the center of the protein not in contact with water |
| disulfide bridges | covalent bonds: two cysteine monomers( have aulfhydryl groups on their side chains) are brought close by folding of the proteinsCH2-S-S-CH2 |
| quatrenary structure | structure that resultspolypeptide chains, or chains. look on pg 83 |
| sickle cell disease | substitution for valine where their should be glutamic acid in the primary structure of homoglobinsickle cell crisis when the wierd shaped blood cells cause clots |
| x ray crystallography | a technique that depends on the diffraction of an x ray beam bythe individual atoms of a crystilized molecule to study the 3D structure of the molecule |
| gene | unit of inheritance,DNA is made up of genes |
| nucleic acids | DNA, RNA |
| deoxyribonucleic acid | provides direction for its replication, directs rna |
| RNA | protein synthesis(ribosomes), mRNA directs protein synthesis to direct production of polypeptides |
| polynucleotides | nucleic acids that exist as polymers. monomers are nucleotides(nitrogenous base,5carbon sugar,phosphate group) |
| pyrimidine | 6 membered ring of carbon and nitrogen atoms. Members:cytosine, thymine, uracil(RNA bonds with A) |
| purine | 5 membered ring, adenine and guanine |
| ribose | sugar connected to the nitrogenous base in RNA |
| deoxyribose(lacks oxygen on carbon) | sugar connected to the nitrogenous base in DNA |
| Protein Structure: Primary | unique amino acids and genes. long chain |
| Protein Structure: Secondary | coils and folds. Hydrogen bonds between the polypeptide backbone bones. O and N atoms of the backbone have a partially negative charge |
| helix(secondary structure) | coil held by H bonds every 4th amino acid |
| pleated sheet(secondary structure) | 2 or more regions in the polypeptide chain lying side by side are connected by H bonds between parts of the two parrallel polypeptide backbones |
| tertiary structure | shapes the protein-determined by side chains of amino acids |
| hydrphobic interaction(tertiary stucture) | polypeptide folds, hydrphobic(nonpolar) side chains clusterin the center of the protein not in contact with water |
| disulfide bridges | covalent bonds: two cysteine monomers( have aulfhydryl groups on their side chains) are brought close by folding of the proteinsCH2-S-S-CH2 |
| quatrenary structure | structure that results polypeptide chains, or chains. look on pg 83 |
Created by:
Megan Fitz
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