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| 12111398237 | Proteins | What is the most abundant biomolecule in the body? | 0 | |
| 12111416769 | Glycine | What is the only amino acid that lacks a chiral center? | 1 | |
| 12111422268 | C-terminal | What part of the amino acid contains a carboxylic acid? | 2 | |
| 12111427364 | N-terminal | What part of the amino acid contains an amine group? | 3 | |
| 12111435971 | L-chiral | What type of chirality has a CRN clockwise arrangement? | 4 | |
| 12111451559 | D-chiral | What type of chirality has a CRN counterclockwise arrangement? | 5 | |
| 12111458271 | Racemic | If the chiral center is a 50-50 mixture of L and D it is referred to as what? | 6 | |
| 12111468811 | L-chiral | Alanine has what chirality? | 7 | |
| 12111479144 | Alanine | Which amino acid functions to make new glucose? (Gluconeogenesis) | 8 | |
| 12111530151 | Aliphatic | What is the term for an R group that contains a hydrocarbon? | 9 | |
| 12111564989 | Leucine | Which amino acid is metabolized into the cholesterol precursor HMG CoA? | 10 | |
| 12111583033 | Valine | Which amino acid is responsible for the improper folding of red blood cells? | 11 | |
| 12111588839 | Hemoglobin | Valine replaces glutamate and causes improper folding in what structure of a red blood cell? | 12 | |
| 12111601438 | Maple Syrup Urine Disease | What disorder occurs when infants are unable to metabolize branched chain amino acids? | 13 | |
| 12111620655 | Sickle cell anemia | What genetic mutation occurred in order to prevent malaria, but causes improper folding of RBC's? | 14 | |
| 12111640071 | Methionine | Which amino acid contains a sulfur and is a precursor for a very import myelinating molecule? | 15 | |
| 12111652511 | Proline | Which amino acid disrupts a-helix and B-pleated sheet formations in secondary structure folding of proteins? | 16 | |
| 12111676928 | Phenylalanine | Which amino acid is a precursor for tyrosine? | 17 | |
| 12111683899 | Phenylketonuria (PKU) | What disorder is a result of decreased metabolism for the amino acid phenylalanine? | 18 | |
| 12111698380 | Tryptophan | Which amino acid is a precursor for serotonin, melatonin, and niacin? | 19 | |
| 12111705402 | Tyrosine | Which amino acid is a precursor for thyroxine and is very important to the beginning pathways of cell signaling? I.e- RTK pathways | 20 | |
| 12111725109 | Very low protein | What should someone with PKU ingest in their diet? | 21 | |
| 12111731353 | Cystic Fibrosis | What is the most common genetic disorder? | 22 | |
| 12111749106 | Serine and threonine | Which amino acids main function is to H bond to other molecules in protein regulation pathways? | 23 | |
| 12111766687 | Cysteine | Which amino acid contains a thiol (SH group) that acts as an antioxidant? | 24 | |
| 12111780794 | Glutamine | Which amino acid is the main nitrogen carrier and is primarily synthesized in the brain? | 25 | |
| 12111795037 | Histimine | What molecule is important for its buffering capacity in hemoglobin? | 26 | |
| 12111835933 | Hydroxylysine | Which amino acid derivative is found in collagen? | 27 | |
| 12111841904 | Isoelectric point | When are amino acids least soluble? | 28 | |
| 12111852917 | pK1 | Which pK is a measure of the dissociation of the carboxylic acid group (C-terminal) on an AA? | 29 | |
| 12111865757 | pK2 | Which pK is referring to the amine group of an AA? | 30 | |
| 12111871070 | pKR | Which pK is referring to the dissociation of protons from the R group on an amino acid? | 31 | |
| 12111886957 | Zwitterion | What is the term that describes the net neutrality of an amino acid? | 32 | |
| 12111903668 | Isoelectric point (pI) | What is the point where an AA or protein is a zwitterion (neutral)? | 33 | |
| 12111911098 | net positive | What is the charge when pH | 34 | |
| 12111919626 | Net negative | What is the charge when pH>pI? | 35 | |
| 12112091397 | Dehydration reactions | What type of reaction is involved in the synthesis of ALL macronutrients? | 36 | |
| 12112119951 | Glutathione | What is the smallest peptide? | 37 | |
| 12112124426 | pKR | Which pK group is the most important group for buffers? | 38 | |
| 12112134821 | Conjugated proteins | What is a protein that has chemical constituents? i.e- glycoproteins and metalloproteins | 39 | |
| 12112155246 | Conformation | What is the spatial arrangement of atoms within a protein? | 40 | |
| 12112159237 | Native conformation | What is it called when a protein is in its most stable, functional conformation? | 41 | |
| 12112198692 | Hydrophobic | What type of amino acids are buried in the middle of a structure, away from water? | 42 | |
| 12112208272 | Primary | What level of protein structure is just the order in which amino acids are aligned? | 43 | |
| 12112222295 | Secondary | What level of structure contains a-helix, B-sheets, and B-turns? | 44 | |
| 12112244829 | Beta turns | What reverses the direction of polypeptides from parallel to anti-parallel? | 45 | |
| 12112280593 | Quaternary | What level of structure consists of two or more polypeptide strands that fold over and bond by non-covalent interactions? i.e- hemoglobin | 46 | |
| 12112295575 | Primary and tertiary | Which levels of structure use covalent (true) bonds? | 47 | |
| 12112303110 | Four | How many different polypeptide strands make up hemoglobin? | 48 | |
| 12112310608 | Fibrous | What type of protein contains a single secondary structure, and functions to provide support? | 49 | |
| 12112319463 | Globular | What type of proteins have several secondary structures and make up enzymes? | 50 | |
| 12112336039 | Glycine | What AA does collagen have the most of? | 51 | |
| 12112344264 | Triple helix | What type of structure is collagen? | 52 | |
| 12112348972 | Scurvy | What disorder occurs from a lack of vitamin C? | 53 | |
| 12112355337 | Vitamin C | What is required for hydroxylation of proline and lysine in collagen synthesis? | 54 | |
| 12112374068 | Posttranslational modification | What is the term that describes the addition of a functional group after the protein is synthesized? | 55 | |
| 12112388002 | Proline hydroxylase and lysyl hydroxylase | What requires vitamin C to add a hydroxyl group to proline and lysine? | 56 | |
| 12112420064 | Lysyl oxidase | What compound deaminates lysine and forms a reactive aldehyde? | 57 | |
| 12112427164 | Copper (Cu) | What is lysyl oxidase dependent upon? | 58 | |
| 12112436447 | Matrix metalloproteins (MMP's) | What degrades collagen? | 59 | |
| 12112452166 | Motif | What pattern of folding is not inherently stable? | 60 | |
| 12112455830 | Domain | What is the part of a polypeptide chain that is independently stable? | 61 | |
| 12112501064 | Entropy (S) | As a protein is folded what decreases? | 62 | |
| 12112529158 | Chaperones | What are the molecules that assist in the folding of proteins? | 63 | |
| 12112563003 | Degraded or accumulated | What happens to a protein if it misfolds? | 64 | |
| 12112579913 | Proteostasis | What process controls protein synthesis, folding, refolding, and degradation of proteins? | 65 | |
| 12112647689 | Globular proteins | What type of proteins are easily denatured? | 66 | |
| 12112657438 | intrinsically unstructured proteins (IUPs) | What is a protein that has no specific structure on at least part of it? | 67 | |
| 12112666903 | Signaling pathways | What are IUP's important for? | 68 | |
| 12112678124 | Metamorphic proteins | What are proteins that are able to form multiple structures that all have different functions? | 69 | |
| 12112729253 | Ligand | What are molecules that are reversibly bound by a protein? | 70 | |
| 12112740343 | Induced fit | What is the structural adaptation of a protein in which a conformational change occurs for the the binding of a ligand? | 71 | |
| 12112759677 | One | How many oxygens can myoglobin carry? | 72 | |
| 12112763504 | Four | How many oxygens can hemoglobin carry? | 73 | |
| 12112771735 | One | If a protein has one polypeptide strand (heme), how many oxygens can it carry? | 74 | |
| 12112789336 | Relaxed | If a hemoglobin is acting as oxyhemoglobin and has a high affinity for binding oxygen, it is in which state? | 75 | |
| 12112835450 | Tense | If a hemoglobin is acting as deoxyhemoglobin and has a low affinity for binding oxygen, it is in what state? | 76 | |
| 12112849693 | Cooperative binding | What term describes the ability of oxygen to bind as more oxygen binds in a hemoglobin? | 77 | |
| 12112864565 | High and easy | What is the affinity for oxygen to bind to a hemoglobin if the hemoglobin already has three O2 bound? How difficult will it be for the last oxygen to bind? | 78 | |
| 12112953203 | Allosteric | If interactions of compounds affect the ability of heme groups to bind oxygen, it is said to be what? | 79 | |
| 12112983534 | Deoxyhemoglobin (tense) | A decrease in pH shifts the hemoglobin towards what state? | 80 | |
| 12112988049 | Oxyhemoglobin (relaxed) | An increase in pH shifts the hemoglobin towards what state? | 81 | |
| 12113032371 | Low affinity | Is affinity for oxygen high or low in peripheral tissues? | 82 | |
| 12113050641 | Carbon monoxide (CO) | What has a 250 times higher affinity to bind to iron in hemes than oxygen? | 83 | |
| 12113073308 | Doesn't allow for release of O2 in tissues | What effect does CO have on the oxygen in hemoglobin? | 84 | |
| 12113084056 | Hemolytic and obstructive | What are the types of jaundice? | 85 | |
| 12113105859 | Hemolytic | Wha type of jaundice has high levels of unconjugated bilirubin? | 86 | |
| 12113115769 | Obstructive | What type of jaundice is able to excreted in the kidneys and has high levels of conjugated bilirubin? | 87 | |
| 12113148859 | IgG | What class of immunoglobulins is most common? | 88 | |
| 12113152095 | IgA | What class of immunoglobulins is found in secretions (tears, saliva, breastmilk)? | 89 | |
| 12113157096 | IgE | What immunoglobulin is the main antibody produced in response to food allergies? | 90 | |
| 12113167194 | IgM | What immunoglobulin is the first antibody produced during an immune response? | 91 | |
| 12113697907 | Speed up reactions | What is the primary function of an enzyme? | 92 | |
| 12113702873 | No | Are enzymes consumed in a reaction? | 93 | |
| 12113706239 | Cofactor | What is the inorganic component of an enzyme? | 94 | |
| 12113709064 | Coenzyme | What is the organic component of an enzyme? | 95 | |
| 12113723612 | Vitamins | What are often used as coenzymes ? | 96 | |
| 12113739639 | Apoenzyme | What is the protein part of an enzyme? | 97 | |
| 12113758803 | Holoenzyme | What is the complete, active enzyme called? (The "whole" enzyme) | 98 | |
| 12113773766 | Zymogen | What is the inactive enzyme precursor called? | 99 | |
| 12113782312 | End in "-ogen" or begin with "pro" | How do you distinguish an inactive enzyme from an active one? | 100 | |
| 12113800619 | Oxidoreductase | What class of enzymes involves the addition or removal of H+? REQUIRES NAD+ or FAD | 101 | |
| 12113816026 | Transferase | What class of enzymes involves the transfer of a functional group? Will often involve ATP, ending with a phosphate being bound to the product | 102 | |
| 12113829485 | Two | How many reactants and products will be involved in transferase? | 103 | |
| 12113840816 | Isomerase | What class of enzymes rearrange functional groups on one molecule? Only involves one reactant and one product | 104 | |
| 12113853237 | Hydrolase | What class of enzymes causes hydrolysis to break bonds? Water is a reactant. | 105 | |
| 12113859983 | Lyase | What class of enzymes cleaves C-C, C-S, or C-N bonds ? | 106 | |
| 12113868736 | Ligase | What class of enzymes is the only class that involves the formation of bonds, and typically uses ATP, but results in a free phosphate group? | 107 | |
| 12113988606 | Active site | What is the part of an enzyme that contains a binding site and a catalytic site? | 108 | |
| 12114023448 | induced fit | Which active site model is the most common and allows for the enzyme to "mold" into a form where the substrate can bind? | 109 | |
| 12114045305 | Binding energy | What is the energy released through the formation of weak bonds in the active site? | 110 | |
| 12114078828 | KM | What is equal to one half of V Max? | 111 | |
| 12156291279 | Vo is dependent on [S] | What happens if [S]< | 112 | |
| 12156302631 | Vo is dependent on both [E] and [S] | What happens if [S]>Km? | 113 | |
| 12156316490 | Vo is dependent on [E], enzyme is saturated with S | What happens if [S]>>Km | 114 | |
| 12156346340 | 1/Vmax | What is the y-intercept of a line weaver burke plot? | 115 | |
| 12156355463 | -1/Km | What does the x-intercept of a Lineweaver-Burk plot represent? | 116 | |
| 12156363077 | Km/Vmax | What is the slope of a lineweaver burke plot? | 117 | |
| 12156387957 | The number will be bigger | What will happen if the line is closer to the origin of a lineweaver burke plot? | 118 | |
| 12156404528 | [E] | What does velocity of enzyme and substrate reactions depend on? | 119 | |
| 12156415599 | Decrease enzyme activity | What happens if there is a deficiency in vitamins or minerals? | 120 | |
| 12156426734 | Increase in rate | What happens to the enzyme if there is an increase in temperature? | 121 | |
| 12156445214 | pH 1.5 | What is the optimum pH of pepsin? | 122 | |
| 12156449814 | pH 6.2 | What is the optimum pH of sucrase? | 123 | |
| 12156452882 | pH 6 | Wha tis the optimum pH of polyphenol oxidase? | 124 | |
| 12156463340 | Denaturation of the enzyme | What will extreme temperatures and pH do to the enzyme? | 125 | |
| 12156475563 | Covalent bonds | What type of bond is in irreversible inhibitor reactions? | 126 | |
| 12156480612 | Noncovalent bonds | What kind of bond is in reversible inhibitor reactions? | 127 | |
| 12156494344 | Active site | Where will a competitive inhibitor bind to? | 128 | |
| 12156505301 | Increased Km and no change in Vmax | What effect does a competitive inhibitor have on Km and Vmax? | 129 | |
| 12156530563 | Only binds the complex | What will an uncompetitive inhibitor bind to? | 130 | |
| 12156541814 | Decreases Km and decreases Vmax | What effect does the uncompetitive inhibitor have on the Km and Vmax? | 131 | |
| 12156569456 | Active site or complex | What will the noncompetitive inhibitor bind to? | 132 | |
| 12156580157 | Decreases Vmax and doesn't change Km | What is the effect of the noncompetitive inhibitor on Km and Vmax? | 133 |
