1. RNA polymerase Enzyme that facilitates transcription 2. Transcription synthesis of an RNA molecule from a DNA template 3. Ribosome Large
... [Show More] macromolecular complex where pro- teins are synthesized 4. tRNA (transfer RNA) Form of RNA that is complementary to mRNA. Has a neucleotide anticodon on one end and an amino acid in the other. 5. Translation decoding of a mRNA message into a polypep- tide chain 6. Coding strand (DNA) The original strand off which the new nu- cleotide sequence is based. Almost the same as mRNA 7. template strand (DNA) The strand mRNA uses to make a copy. Complementary to mRNA 8. missense mutation base substitution results in change in an amino acid 9. nonsense mutation changes a normal codon into a stop codon 10. silent mutation change in DNA that codes for the same amino acid 11. Replication process of copying DNA prior to cell division 12. DNA polymerase III synthesizes new DNA only in the 5' to 3' di- rection Needs a primer to start 13. polymerase chain reaction (PCR) Copying DNA in lab. Used to study/diagnose 14. PCR needs Target DNA dNTPs (deoxyneucleotides) DNA primers Taq polymerase (stable at high temps) 15. Helicase An enzyme that untwists the double helix of DNA at the replication forks. 16. Ligase An enzyme that connects two fragments of DNA to make a single fragment 17. Repair for damage to bases from harmful molecules (like chemicals) Base excision (removes damaged base and replaces it) 18. Mismatch repair Repair for base mismatches due to errors in replication 19. Repair for double stranded breaks in DNA (Radiation/x-rays) Homologous recombination (using sister chromosome as model) Non homologous end joining (no model avail- able) 20. Nucleotide excision Repair for damage from UV which causes ad- jacent nucleotides to fuse together (thiamine dimers) 21. Amino acid sequence wraps around proteins called Histones 22. Histones organize to form Nucleosomes 23. Nucleosomes organize to form Chromatin 24. Chromatin organizes to form A chromosome 25. Complete dominance When the phenotypes of the heterozygote and dominant homozygote are indistinguish- able. 26. Codominance A condition in which neither of two alleles of a gene is dominant or recessive. Both phenotypes are expressed. 27. Incomplete dominance when the phenotypes of the two alleles blend 28. Point mutations chemical changes in just one base pair of a gene 29. frameshift mutations Insertions and deletions 30. 4 parts of an amino acid Carboxyl group Alpha carbon Amino group R side chain 31. COO- I H - C - R I NH3+ Abbreviated structure (amino acid) 32. 3 types of amino acids Hydrophobic Polar Charged 33. Bonds in hydrophobic amino acids C-C, C-H 34. Bonds in polar amino acids O-H N-H S-H 35. Primary protein structure Sequence of amino acids form peptide bonds 36. Secondary protein structure Hydrogen bonding of the peptide backbone causes amino acids to fold into a repeating pattern 37. tertiary protein structure 3-D folding pattern of a protein due to side chain interactions 38. Quaternary protein structure Protein consisting of more than one amino acid chain 39. hydrophobic interactions Weak interactions between amino acids in a protein that come together to avoid water and can be disrupted by heat 40. 2 types of bonds in polar in- teractions Hydrogen bonds Disulfide bonds 41. Hydrogen bond Weak bond where hydrogen from a polar amino acid attracts an electronegative atom like O & N. Can be disrupted by heat and change in pH. 42. Disulfide bond Very strong covalent bond between two sul- fur atoms. Can only be broken by chemical agents. 43. Ionic bonds Bonds in charged interactions between +R group and -R group. Moderately strong, can be broken by change in pH or by salts. 44. Dehydration reaction Creates a peptide bond by removing water. 45. Hydrolysis Breaking peptide bonds by adding water. 46. protein phosphorylation The attachment of a phosphate group of a polar amino acid group. 47. Protein dephosphorylation Removal of a phosphate group of a polar amino acid. 48. competitive inhibitor A molecule similar to a substrate that can bind to the enzymes active site. Reversible Increased substrate=increase in reaction 49. Non competitive inhibitors A molecule that binds to a place on the en- (allosteric) zyme other than the active site that changes the shape of the enzyme which interferes with the binding of the substrate. Some reversible, some permanent. Increased substrate does not = increased re- action 50. Feedback inhibition When end product is no longer being con- sumed and starts accumulating, the end product binds with the initial enzyme, stop- ping it from bonding with the substrate. Reversible 51. Ways to target enzymes in Modify diet (like HFI-removing fructose from disease diet) Enzyme therapy (like CF to increase digestive enzymes) Drugs that increase substrate of an en- zyme(like Parkinson's with LDopa) Drugs that inhibit enzyme activity (like viagra) 52. Myoglobin affinity and loca- High O2 affinity, stores O2 in muscles tion 53. Hemoglobin affinity and lo- Lower O2 affinity, picks up O2 in lungs and cation delivers to body 54. Myoglobin structure 1 protein subunit (1 heme group and 1 iron) 55. Hemoglobin structure 4 protein subunits 56. Cooperativity In Hgb, if 1 heme gets filled the other 3 want to get filled. If 1 O2 leaves, the others tend to leave. 57. Hemoglobin in the lung -5 qualities 58. Hemoglobin in muscle-5 qualities Higher O2 affinity Relaxed state Higher pH Low CO2 Low H+ Lower O2 affinity Tense state Lower pH High CO2 Lots of H+ 59. The Bohr effect The difference of O2 affinity at different pH Shift to left= in higher pH- higher affinity Shift to right= in lower pH- lower affinity 60. sickle cell anemia cause A mutation in the beta subunit of hemoglobin which leads to insertion of valine into the hy- drophobic patches on deoxygenated Hgb. 61. ATP Molecule that fuels our body's activity 62. 3 major steps in aerobic me- tabolism Glycolysis Citric acid cycle (CAC) or Kreb's cycle Electron transport chain (ETC) 63. Inputs of cellular respiration O2 and sugar 64. Outputs of cellular respira- tion CO2, H2O, ATP 65. Cellular respiration The process our bodies use to convert food to energy. 66. Mitochondria Organelle of a cell where much of cellular respiration occurs. 67. Glycolysis location Cytoplasm 68. Glycolysis inputs Glucose 2 ATP 4 ADP 2 NAD+ 69. Glycolysis outputs 2 pyruvate 2 NADH 4 ATP 2 ADP 70. Pyruvate moves into the and is converted to . 71. Citric acid/ Krebs cycle loca- tion 72. Citric acid/ Krebs cycle in- puts 73. Citric acid/ Krebs cycle out- puts 74. Electron transport chain lo- cation 75. Electron transport chain in- puts 76. Electron transport chain out- puts Matrix, Acetyl CoA Matrix Acetyl CoA NAD+ GDP FAD CO2 NADH GTP FADH2 Inner membrane NADH FADH2 O2 ADP + P NAD+ FAD H2O ATP 77. At the end of the ETC, ATP is formed when 78. What occurs when no O2 is present? 79. Fermentation converts into . 80. What happens in the Cori cy- cle? 81. Cori cycle has a net loss of . Protons (H+) in the intermembrane rush through ATP synthase in the inner membrane and into the matrix. ETC cannot occur. Instead fermentation hap- pens. NADH, NAD+ and 2 lactates Fermentation To liver where 2 lactates are converted to glucose using 6 ATP Glucose goes back into blood stream and to cells. 4 ATP 82. Glut 4 Cell doorways for glucose. 83. Insulin the Glut4 doors. 84. Glucagon the Glut4 doors. Opens Closes 85. Glycogenesis Glucose forms a chain called glycogen. Happens in the liver when it detects insulin. 86. Glycogenolysis Break down of glycogen to glucose to be re- leased into blood stream. Happens in liver when it detects glucagon. 87. In diabetes, glucose and pro- tein do what? Bond to form a glycated protein. Glycated pro- teins aggregate to form Advanced Glycation End Products (AGEs) [Show Less]