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| 1778363779 | Macromolecules | polymers built from monomers Carbohydrates Proteins Nucleic Acids | 0 | |
| 1778363780 | Carbohydrates | serve as fuel and building material | 1 | |
| 1778363781 | Lipids | diverse group of hydrophobic molecules one class of large biological molecules that do not form | 2 | |
| 1778363782 | Proteins | include a diversity of structures, resulting in a wide range of functions | 3 | |
| 1778363783 | Nucleic acids | store, transmit, and help express hereditary and application polymers made of monomers called nucleotides | 4 | |
| 1778363784 | 4 important large molecules | carbohydrates lipids proteins nucleic acid | 5 | |
| 1778363785 | alcohol dehydrogenous | breaks down alcohol in the body | 6 | |
| 1778363786 | polymers | long molecules consisting of many similar or identical building blocks linked by covalent bonds | 7 | |
| 1778363787 | monomers | repeating units that serve as building blocks of a polymer | 8 | |
| 1778363788 | enzymes | specialized macro-molecules that speed up chemical reactions | 9 | |
| 1778363789 | dehydration reaction | reaction in which two molecules are covalently bonded, with the loss of a water molecule | 10 | |
| 1778363790 | hydrolysis | process that is the reverse of dehydration reaction water breakage bond between monomers is broken by the addition of a water molecule | 11 | |
| 1778363791 | Carbohydrates | sugars and polymers of sugars | 12 | |
| 1778363792 | Monosaccharides | simple sugars CH2O | 13 | |
| 1778363793 | Trioses | 3 - carbon sugars C3H6O3 | 14 | |
| 1778363794 | Pentoses | 5 - carbon sugars C5H10O5 | 15 | |
| 1778363795 | Hexoses | 6 - carbon sugars C6H12O6 | 16 | |
| 1778363796 | Disaccharide | two monosaccharides joined by glycosidic linkage | 17 | |
| 1778363797 | glycosidic linkage | covalent bond between two monosaccharides by a dehydration reaction | 18 | |
| 1778363798 | polysaccharides | macro-molecules storage material, hydrolyzed as needed to provide sugar for cells, building material for structures that protect the cell or the whole organism | 19 | |
| 1778363799 | starch | polymer of glucose monomers stored as granules within plastids represent stored energy withdrawn by hydrolysis | 20 | |
| 1778363800 | glycogen | polysaccharide glucose that is like amylopectin but more intensely branched | 21 | |
| 1778363801 | cellulose | major component of tough walls that enclose plant cells aids in poop | 22 | |
| 1778363802 | starch molecules | largely helical | 23 | |
| 1778363803 | cellulose molecule | straight never branched | 24 | |
| 1778363804 | microfibrils | parallel cellulose molecules held together by hydrogen bonds | 25 | |
| 1778363805 | chitin | carbohydrates used by arthropods (insects) to build their exoskeletons | 26 | |
| 1786661424 | polymer | hydrophobic consist of mostly hydrocarbons from non-polar bonds | 27 | |
| 1786661425 | fats | constructed from two types of smaller molecules: gylcerol and fatty acids energy storage stored in Adipose cells | 28 | |
| 1786661426 | fatty acid | carboxyl group with long carbon skeleton | 29 | |
| 1786661427 | saturated fatty acids | maximum number of hydrogen atoms possible and double bonds | 30 | |
| 1786661428 | triacylgecerol | 3 fatty acids linked to one glycerol molecule | 31 | |
| 1786661429 | trans fat | hydrogenation of unsaturated to saturated | 32 | |
| 1786661430 | phospholid | two fatty acids and an phosphate group are attached to gylcerol hydrophobic form bilayer cell makes wall | 33 | |
| 1786661431 | steroids | carbon skeleton consisting of four fused rings | 34 | |
| 1786661432 | cholesterol | important steroid | 35 | |
| 1786661433 | catalyst | chemical agents that selectively speed up chemical reactions without being consumed by the reaction | 36 | |
| 1786661434 | polypeptide | bond between amino acids called a peptide bond A polymer of amino acids | 37 | |
| 1786661435 | protein | biologically functional molecule made up of one or more polypeptides, folded and coiled into a specific three-dimensional structure | 38 | |
| 1786661436 | amino acid | an organic molecule with both an amino group and a carboxyl group | 39 | |
| 1786661437 | Enzymatic proteins | protein function selective acceleration of chemical reactions | 40 | |
| 1786661438 | Storage Proteins | protein function storage of amino acids | 41 | |
| 1786661439 | Hormonal Proteins | protein function coordination of an organisms activities | 42 | |
| 1786661440 | contractile and motor proteins | protein function aids in movement | 43 | |
| 1786661441 | Defensive Proteins | protein function protection against disease | 44 | |
| 1786661442 | Transport Proteins | protein function Transport of substances | 45 | |
| 1786661443 | Receptor Proteins | protein function response of cell to chemical stimuli | 46 | |
| 1786661444 | Structural Proteins | protein function support | 47 | |
| 1786661445 | peptide bond | covalent bond resulting from two amino acids joined by dehydration reactions yield a polypeptide | 48 | |
| 1786661446 | polypeptide backbone | repeating sequence of atoms | 49 | |
| 1786661447 | Primary Structure | Linear chain of amino acids dictates secondary and tertiary structure due to the chemical nature of the backbone and the side chains of the amino acids along the polypeptide has a carboxyl end | 50 | |
| 1786661448 | Secondary Structure | regions stabilized by hydrogen bonds between atoms of the polypeptide backbone | 51 | |
| 1786661449 | helix | ⍺ a delicate coil held together by hydrogen bonding between every fourth amino acid | 52 | |
| 1786661450 | pleated sheet | β two or more segments of the polypeptide chain lying side by side are connected by the hydrogen bonds between parts of the two parallel segments of the polypeptide backbone | 53 | |
| 1786661451 | Tertiary Structure | three-dimensional shape stabilized by interactions between side chains overall shape of the polypeptide resulting from interactions between the side chains of the various amino acids | 54 | |
| 1786661452 | hydrophobic interactions | misleading amino acids with hydrophobic side chains usually end up in clusters at the core of the protein out of contact with water caused by the exclusion of nonpolar substances by water molecules | 55 | |
| 1786661453 | disulfide bridges | covalent bonds that reinforce the shape of a protein form where two cysteine monomers are brought close together by the folding of the protein | 56 | |
| 1786661454 | Quaternary Structure | association of two or more polypeptides (some proteins only) overall protein structure that results from the aggregation of these polypeptide subunits | 57 | |
| 1786661455 | collagen | fibrous proteins that has three identical helical polypeptides intertwined into a larger triple helix giving the long fibers great strength | 58 | |
| 1786661456 | hemoglobin | oxygen-binding protein of red blood cells protein that carries oxygen in red blood cells | 59 | |
| 1786661457 | sickle-cell disease | inherited blood disorder caused by the substitution of one amino acid for the normal one at a particular position in the primary structure of hemoglobin | 60 | |
| 1786661458 | denaturation | protein unraveling and losing its native shape transferred from an aqueous environment to a nonpolar solvent agents that disrupt the hydrogen bonds, ionic bonds, and disulfide bridges that maintain proteins shape excessive heat | 61 | |
| 1786661459 | chaperonins | assist in the proper folding of the protein DO NOT specify the final structure of a polypeptide keep the polypeptide segregated from disruptive chemical conditions in the cytoplasmic environment while it folds spontaneously provides a shelter for folding polypeptides | 62 | |
| 1786661460 | X-ray crystallography | determine the 3D structure of many other proteins | 63 | |
| 1786661461 | bio-informatics | predict structure from their amino acid sequence | 64 | |
| 1786661462 | gene | unit of inheritance | 65 | |
| 1786661463 | ribosomes | site of protein synthesis between nucleus and the plasma membrane | 66 | |
| 1786661464 | polynucleotides | nucleic acids are macromolecules that exist as polymers | 67 | |
| 1786661465 | nucleotides | composed of 5 carbon sugars (pentose), nitrogen-containing base, and one or more phosphate groups | 68 | |
| 1786661466 | nucleoside | portion of a nucleotide without any phosphate group | 69 | |
| 1786661467 | pyrimidine | one six-membered ring of carbon and nitrogen atoms cytosine, thymine, uracil | 70 | |
| 1786661468 | purines | larger than pyrimidine six-membered ring fused to a five-membered ring adenine, guanine | 71 | |
| 1786661469 | deoxyribose | DNA sugar to which the nitrogenous base is attached | 72 | |
| 1786661470 | Ribose | RNA sugar to which the nitrogenous base is attached | 73 | |
| 1786661471 | sugar-phosphate backbone | bonding result in a repeating pattern of sugar-phosphate units | 74 | |
| 1786661472 | double helix | two "strands" winding around an imaginary axis | 75 | |
| 1786661473 | antiparallel | opposite 5' -> 3' directions from each other | 76 | |
| 1786661474 | DNA sequencing | determining the sequence of nucleotides along a DNA strand | 77 | |
| 1786661475 | genomics | study of genes | 78 | |
| 1786661476 | proteomics | analysis of large sets of proteins including their sequences | 79 |
