Biochemistry WGU

1. semi conservative DNA replication is , meaning that each new duplex has one original (parent) strand and one new strand. 2. template Because the two parent strands are separated during replication and the base pairing is predictable, each parent strand can serve as a for the new strand synthesis. 3. helicase unwinds the double stranded DNA to allow for replica- tion, but this is not a problem for the DNA polymerase. 4. Nucleotide excision is used to repair deletions, inser- repair 5. complementary strand 6. complementary se- quence 7. mRNA DNA se- quence tions, and helix-distorting lesions, such as thymine dimers. a strand of DNA that is the exact match of another Nucleic acid base sequences that can form a dou- ble-stranded structure by matching base pairs. The use of U instead of A, starts from right to left. 8. 32 How many DNA copies after 4 complete PCR cycles? 9. DNA polymerase This recognizes the primers and uses the available dNTPS to replicate the template DNA sequence. 10. nonsense mutation 11. missense mutation 12. frameshift mutation 13. silent mutation 14. x linked recessive 15. autosomal dominant 16. autosomal recessive 17. x linked dominant 18. SIRT1, SIRT2 associated with chronic exposure to cocaine and drug addiction, the nucleosomes become widely spaced. 19. alternative splicing of mRNA Alternative combination of exons within the same gene are linked together. 20. base excision repair -nucleotide is cut out and replaced with correct nu- cleotide 21. recombination the exchange of genetic material between homolo- gous chromosomes, resulting from a cross-over event 22. nucleotide excision repair a nuclease cuts out and replaces damaged stretches of DNA 23. mismatch repair the cellular process that uses specific enzymes to remove and replace incorrectly paired nucleotides 24. xeroderma pigmen- tosum 25. amino group 26. carboxyl group 27. side chain 28. alpha carbon 29. hydrogen bond 30. ionic bond 31. hydrophobic effect The is the primary "force" of protein structural stabilization. 32. hydrogen bonding bond connecting the nitrogenous bases (A, T, G, C) 33. electrostatic interac- tions 34. disulfide bonding What binds the enzyme and substrate with the active site? (hint: type of interaction) salt bridges 35. tertiary structure 36. glycogen depletion An unwanted effect of an overly vigorous warm-up is: 37. protein aggregation causes Alzheimer disease 38. carbohydrate catab- olism breakdown of carbohydrate molecules to produce en- ergy, glycolosis, krebs cycle, ETC 39. PKU 40. primary structure The level of protein structure referring to the specific sequence of amino acids, established through the dehydration synthesis of peptide bonds. 41. dehydration synthe- sis the process of joining two molecules, or compounds, together following the removal of water 42. peptide bonds Bonds between amino acids 43. acidic amino acid negatively charged, aspartame and glutonate 44. hemoglobin blood protein containing iron; carries oxygen in red blood cells 45. high ph, low carbon dioxide oxygenated form of hemoglobin 46. binding curves 47. ph affinity Which feature of hemoglobin makes it an effective oxygen transport? 48. Binds to excess H How does hemoglobin keep blood PH neutral during exercise? 49. carbon dioxide de- creases What is occurring in surrounding tissues as the amount of hemoglobin saturated with oxygen increas- es? 50. phosphorylation What is a temporary modification to a protein struc- ture by kinases that alters enzyme function? 51. methylation a biochemical process that influences behavior by suppressing gene activity and expression 52. Acetylation gene activation 53. carboxylation a type of condensation reaction where a carboxyl group is added to another molecule 54. substrate concentra- tion enzyme activity increases as this increases 55. catalyzed reactions the reactants of enzyme that bind to sites on the enzyme (called active sites- lock and key) 56. enzyme specificity enzymes are designed to work only on a specific substrate or group of closely related substrates and create one reaction 57. alters enzymes function by changing its shape 58. allosteric site different site on the enzyme where the noncompeti- tive inhibitor binds 59. uncompetitive in- hibitor reversible enzyme inhibitor that binds only to the en- zyme-substrate complex 60. irreversible inhibitor a substance that causes inhibition that cannot be reversed 61. protease An enzyme that digests proteins by hydrolysis. 62. decrease Protease activity would if ph in- creased. 63. enzyme specialized proteins that speed up chemical reactions (specific) 64. feedback inhibition 65. competitive inhibi- tion 66. irreversible inhibi- tion 67. glycogen starch; glucose is stored in the form of glycogen in liver cells 68. triglyceride Circulate in the blood and are made up of three fatty acids attached to a glycerol. 69. sucrose glucose and fructose 70. cellulose polysaccharide that is the major complex carbohy- drate in plant cell walls 71. carbohydrate metab- olism maintains normal blood glucose level 72. insulin Stimulates the uptake of glucose from the blood cells in the body. 73. glyconeogenesis process of producing glucose from fat and protein an amino acid can be used 74. krebs cycle the series of reactions in which pyruvate is broken down into carbon dioxide 75. glycation bonding of a protein or lipid molecule with a sugar, without the controlling action of an enzyme 76. 8 acetyl-CoA 77. beta oxidation involves coenzyme A, NAD, and FAD 78. electron transport chain a series of proteins embedded in the thylakoid mem- brane 79. glycolysis breaks down glucose into two molecules of pyruvate 80. fermentation process by which cells release energy in the absence of oxygen 81. Acetyl-CoA pyruvate directly converted to under aerobic condi- tions 82. ATP (Adenosine triphosphate molecule) main energy source that cells use for most of their work. 83. lactate A product of pyruvate metabolism when oxygen is limited 84. mitochondria Powerhouse of the cell, organelle that is the site of ATP (energy) production, not located in the red blood cells 85. 2 how many molecules of lactate are required to pro- duce one molecule of glucose 86. 6 How many ATP to convert pyruvate to glucose 87. pyruvate Three-carbon compound that forms as an end prod- uct of glycolysis. 88. glucagon a hormone secreted by the pancreas that signals glycogen breakdown. 89. phospholipid 90. cholesterol maintains membrane fluidity 91. doesn't absorb vitamin c phospholipid mi- celles 92. acetone very few carbs and high fats produce this ketone in the blood 93. agouti gene expres- sion 94. oxidation damage base excision repair 95. polar amino side 96. aerobic metabolism the production of energy through the use of oxygen in the cell 97. hydrophobic inter- actions Why does the egg turn white when it is heated? 98. prion disease a disease caused by an abnormal protein particle that infects brain tissue, propagation protein misfolding 99. Bohr Effect An increase in carbon dioxide production leads to a decrease in blood PH, causing hemoglobin to release oxygen more readily. 100. changes structure What happens when you bind a gas to a heme group? 101. Myoglobin has a much larger affinity for o2 than hemoglobin does. 102. ABO blood group a category of blood based upon the presence or ab- sence of two glycolipid antigens, A and B (glycopro- teins) 103. glycolipid A polymer of monosaccarides covalently attached to a membrane lipid. 104. eicosanoids chemical messengers (signals) molecules 105. monosaturated fatty acid 106. omega carbon 107. gylcogenolysis C8H14O2 108. changing the en- zyme's three dimen- sional shape How does heating beyond a optimum temperature inactivate an enzyme? 109. induced fit when a substrate binds to an enzyme, the active site changes shape--like a clasping hand shake 110. PCR steps 1. denaturation 2. annealing 3. elongation 111. epigenetic changes changes in gene expression without changes to the DNA sequence 112. frameshift mutations mutations involving the insertion or deletion of one or more nucleotides in a gene 113. missense mutations replace one amino acid with another 114. nonsense mutations produce a premature stop codon 115. silent mutations Is when a mutation is there, but does not change the normal gene function. 116. Tay sachs an autosomal recessive disease example 117. point mutation gene mutation involving changes in one or a few nucleotides 118. Thymine Dimers bond formed by 2 Thymines in DNA. Caused by UV light, results in mutation or death 119. ionic bonds, hy- drophobic inter- actions, hydrogen bonds, and disulfide bonds. The interactions that stabilize tertiary structure to- gether 120. phosphodiester What type of bond is made between nucleotides? 121. hydrogen bonds between backbone atoms, includes al- pha helices and beta sheets as common forms A secondary structure of protein consists of 122. Chaperones a type of protein that assists in the folding of other molecules 123. substrate reactant to which an enzyme binds 124. kinases What adds phosphates to molecules? 125. phosphatases enzymes that remove phosphate groups 126. coo carboxyl group 127. Replacing a polar amino acid with a non polar amino acid 128. Noncompetitive inhi- bition 129. interior of a protein 130. ionic bond 131. hydrogen bond Which one of the following mutations will likely cause a neurodegenerative disease? When an inhibitor binds reversibly to a site of the en- zyme that is not the active site, what type of inhibition results? 132. dehydration reaction builds a polypeptide 133. hydrolysis breaks down a polypeptide 134. one, four How many subunits do myoglobin and hemoglobin each have? 135. oxygen binding alters the shape of the iron-heme complex, and there- fore its light absorption properties as indicated by a color change. 136. Relaxed or r The oxyhemoglobin conformation is specifically re- ferred to as the state 137. Tense or T the deoxyhemoglobin conformation is referred to as the state. 138. sickle cell In case of , a hydrophilic amino acid-glutamate is re- placed by a non polar-hydrophobic amino acid-valine, leading to polymerization of hemoglobin, fibril forma- tion and eventually sickling of the red blood cells. 139. oxygen When binding hemoglobin or myoglobin, CO binds in place of . 140. amino group 141. carboyxl group 142. high pH,low pH Hemoglobin binds to the oxygen at a and releases oxygen at a . 143. vitamin e Which of the following nutrients cannot be broken down to a substance that can participate in the pro- duction of ATP via aerobic cellular metabolism ? 144. Substrate level phosphorylation Glycolysis produces two ATP molecules. Through what process are these ATP molecules made? 145. Acetyl CoA What product of beta oxidation is able to enter the citric acid cycle? 146. glycolysis What process is shared between anaerobic and aer- obic Metabolism ?