412843208 | polymer | many similar or identical building blocks linked by covalent bonds | 0 | |
412843209 | monomers | building blocks of polymers | 1 | |
412843211 | enzymes | macromolecules that speed up chemical reactions | 2 | |
412843212 | dehydration reaction | two molecules covalently bonded together with the loss of a water molecule | 3 | |
412843213 | dehydration reaction | one monomer provides a hydroxyl group (-OH), while the other provides a hydrogen (-H) | 4 | |
412843214 | hydrolysis | reverse reaction of dehydration | 5 | |
412843215 | hydrolysis | polymers are disassembled to monomers | 6 | |
412843217 | hydrolysis | water breakage | 7 | |
412843498 | protein | build from 20 kinds of amino acids | 8 | |
412843500 | carbohydrates | sugars and polymers of sugars | 9 | |
412843501 | monosaccharides | single sugar | 10 | |
412843502 | hexoses | 6 carbon sugar | 11 | |
412843504 | trioses | 3 carbon sugar | 12 | |
412843505 | pentose | 5 carbon sugar | 13 | |
412843506 | rings | in aqueous solutions, glucose, as well as other five- and six-carbon sugars form | 14 | |
412843508 | disaccharide | two monosaccarhides joined by a glycosidic linkage | 15 | |
412843511 | glycosidic linkage | covalent bond formed between two monosaccarhides by a dehydration reaction | 16 | |
412843512 | maltose | glucose + glucose glycosidic linkage | 17 | |
412843513 | sucrose | glucose + fructose | 18 | |
412843515 | polysaccharides | macromolecules, polymers w/ a few hundred to a few thousand monosaccharides joined by a glycosidic linkage | 19 | |
412843516 | starch | polymer of glucose monomers | 20 | |
412843517 | stored energy | starch | 21 | |
412843518 | amylose | simplest form of starch, unbranched | 22 | |
412843520 | amylopectin | complex form of starch, branched polymer | 23 | |
412843521 | glycogen | a polysaccharide stored by animals | 24 | |
412843522 | glycogen | a polymer of glucose much like amylopectin but more extensively branched | 25 | |
412843523 | type of polysaccharide | cellulose | 26 | |
412843524 | cellulose | most abundant organic compound on earth | 27 | |
412843525 | cellulose | polymer of glucose | 28 | |
412843526 | cellulose | insoluble fiber | 29 | |
412843527 | chitin | carbohydrate used by arthropods to build exoskeletons | 30 | |
412843529 | chitin | structural polysaccharide | 31 | |
412843533 | lipids | biological molecules that does not include true polymers | 32 | |
412843534 | lipids | generally not big enough to be considered macromolecules | 33 | |
412843537 | lipids | mix poorly (if at all) with water | 34 | |
412843540 | lipids | mostly of hydrocarbon regions | 35 | |
412843546 | lipids | waxes | 36 | |
412843549 | fats, phospholipids and steroids | lipids | 37 | |
412843550 | fat | constructed from glycerol and fatty acids | 38 | |
412843551 | fatty acid | long carbon skeleton, usually 16 or 18 carbon atoms length | 39 | |
412843552 | relatively non polar c-h bonds in hydrocarbon chains of fatty acids | why are fats hydrophobic | 40 | |
412843553 | triacyglycerol | three fatty acids linked to one glycerol molecule | 41 | |
412843554 | saturated fatty acid | no double bonds between carbon atoms | 42 | |
412843555 | unsaturated fatty acid | one or more double bonds, with one fewer hydrogen atom on each double-bonded carbon | 43 | |
412843556 | cis | nearly all double bonds in naturally occurring fatty acids are __________ double bonds | 44 | |
412843557 | saturated fat | lard, butter | 45 | |
412843559 | unsaturated fat | olive oil | 46 | |
412843570 | saturated fat | cause of cardiovascular disease known as atherosclerosis | 47 | |
412843572 | energy storage | major function of fats | 48 | |
412843573 | 1g of fat | stores twice as much energy as a gram of a polysaccharide such as starch | 49 | |
412843574 | phospholipid | hydrophilic head and two hydrophobic tails | 50 | |
412843577 | phospholipid | two fatty acids attached to glycerol | 51 | |
412843578 | bilayers | tails of phospholipids facing each other | 52 | |
412843579 | steroid | lipids characterized by a carbon skeleton consisting of four fused rings | 53 | |
412845297 | type of steroid | cholesterol | 54 | |
412845298 | protein | account for 50% of the dry mass of most cells | 55 | |
412845299 | speed up chemical reactions, defense, storage, transport, cellular communication, movement or structure support | roles of a protein | 56 | |
412845300 | regulate metabolism | enzymatic proteins | 57 | |
412845301 | catalyst | chemical agents that speed up chemical reactions WITHOUT being consumed by the reaction | 58 | |
412845302 | protein | constructed from a set of 20 types of amino acids | 59 | |
412845303 | polypeptide | bond of a polymer of amino acids | 60 | |
412845305 | peptide bond | link between amino acids | 61 | |
412845306 | protein | made up of one or more polypeptides | 62 | |
412845307 | amino acid | organic molecule with both an amino group and a carboxyl group | 63 | |
412845308 | R group | side chain within each amino acid | 64 | |
412845309 | globular proteins | spherical proteins | 65 | |
412845311 | fibrous proteins | proteins shaped like long fibers | 66 | |
412845317 | primary, secondary, tertiary | levels of protein structure | 67 | |
412845318 | primary structure | linear chain of amino acids | 68 | |
412845320 | secondary structure | regions stabilized by hydrogen bonds between atoms of the polypeptide backbone | 69 | |
412845321 | alpha helix | coiled secondary structure of a protein | 70 | |
412845322 | beta pleated sheets | make up the core of globular proteins | 71 | |
412845324 | beta pleated sheets | flat secondary structure of a protein | 72 | |
412845328 | tertiary structure | overall shape of a polypeptide | 73 | |
412845329 | hydrogen bond | hydroxyl group (-OH) loses a hydrogen, carboxyl group (C=O) loses an oxygen | 74 | |
412845331 | sulfhydryl groups (-SH) brought close together by the folding of the protein | disulfide bridge | 75 | |
412845333 | hydrophobic interaction | 76 | ||
412845334 | ionic bond | 77 | ||
412845336 | quaternary structure | protein consisting of two or more polypeptide chains aggregated into one functional macromolecule | 78 | |
412845337 | sickle-cell disease | caused by the substitution of one amino acid within the primary structure of hemoglobin | 79 | |
412845338 | denaturation | protein unravels and loses with native shape | 80 | |
412845339 | denaturation | weak chemical bonds and interaction within a protein may be destroyed | 81 | |
412845342 | chaperonins | chaperon proteins | 82 | |
412845343 | chaperonins | protein molecules that assist in the proper folding of other proteins | 83 | |
412845344 | chaperonins | keep a polypeptide segregated from disruptive chemical conditions | 84 | |
412845347 | hydrophilic | chaperonins have a ___________ environment that aids the folding process | 85 | |
412845348 | cystic fibrosis, alzheimer's, parkinson's and mad cow disease | associated with misfolded proteins | 86 | |
412845349 | x-ray crystallography, NMR spectroscopy, bioinformatics | approaches to understanding protein structure and function | 87 | |
412845350 | gene | consist of DNA | 88 | |
412845351 | gene | programs the amino acid sequence of a polypeptide | 89 | |
412845352 | nucleic acids | polymers made of monomers | 90 | |
412845355 | DNA, RNA | two types of nucleic acids | 91 | |
412845356 | DNA | provides directions for its own replication | 92 | |
412845357 | DNA | directs RNA synthesis | 93 | |
412845358 | gene expression | DNA > RNA > amino acids > proteins | 94 | |
412845360 | ribosomes | cellular structure for protein synthesis | 95 | |
412845364 | nucleus | location of DNA | 96 | |
412845383 | polynucleotides | nucleic acids that exist as polymers | 97 | |
412845385 | nucleotide | polynucleotide monomer | 98 | |
412845386 | cytosine | pyrimidine | 99 | |
412845387 | thymine | pyrimidine | 100 | |
412845389 | uracil | pyrimidine | 101 | |
412845846 | adenine | purine | 102 | |
412845849 | guanine | purine | 103 | |
412845850 | deoxyribose | sugar in DNA | 104 | |
412845852 | ribose | sugar in RNA | 105 | |
412845853 | nucleoside | portion of a nucleotide without phosphate groups | 106 | |
412845854 | pyrimidine | single ring base w/in DNA | 107 | |
412846038 | purine | double ring base w/in DNA | 108 | |
412846039 | double helix | polynucleotides that wind around an imaginary axis within DNA | 109 | |
412846040 | antiparallel | opposite 5' - 3' directions sugar phosphate backbones run | 110 | |
412846041 | pairs with adenine | pairs with thymine | 111 | |
412846042 | pairs with cytosine | pairs with guanine | 112 | |
412846044 | tRNA | brings amino acids to the ribosome during synthesis of a polypeptide | 113 | |
412846049 | DNA | bearer of genetic information | 114 | |
673650633 | ester | compound most often formed by the condensation of an alcohol and an acid, by removing water. It contains the functional group carbon-oxygen double bond joined via carbon to another oxygen atom | 115 | |
673650635 | hydrogenation | The chemical reaction of hydrogen with another substance, especially with an unsaturated organic compound, and usually under the influence of temperature, pressure and catalysts | 116 | |
673650638 | enzyme | a globular protein that catalyses a biological chemical reaction | 117 | |
1313872306 | nucleotide | consists of three parts: a nitrogenous base, a pentose sugar, and one or more phosphate groups | 118 | |
587762282 | ATP | consists of a nitrogenous base (adenine), a pentose sugar, and three phosphate groups. | 119 | |
510230310 | proteins, nucleic acids, polysaccharides, and lipids | The four main categories of large biological molecules present in living systems are | 120 | |
970584626 | glycosidic linkage | join simple sugars to form polysaccharides | 121 |
Biology - Campbell 10th Ed Ch 5 Flashcards
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