WGU BioChem OA Review with correct answers
aWGU BioChem OA Review Males and Females are equally affected - correct answer Autosomal The process of copying DNA in the lab. - correct answer Polymerase Chain Reaction (PCR) Template DNA, Nucleotides (dNTPS), DNA Polymerase, and DNA Primers. - correct answer What is needed for Polymerase Chain Reaction? Denaturing, Annealing, Elongating - correct answer What are the three steps of a Polymerase Chain Reaction (PCR)? Denaturing (DNA is heated up to separate it) - correct answer What is the first step of a Polymerase Chain Reaction? Cooling the Polymerase Chain Reaction. Primers stick to the DNA that you want to copy and ADD DNA Polymerase - correct answer What is Annealing? The Polymerase Chain Reaction is heated and DNA Polymerase adds nucleotides to build a new DNA strand. - correct answer What is elongating? Ligase - correct answer What is NOT involved in PCR? It is used to repair damage to bases caused by harmful molecules by removing the base that is damaged and replacing it. #1 GLYCOSYLASES see the damaged DNA. #2 DNA Polymerase puts the right one back #3 DNA Ligase seals it. - correct answer What is base excision repair (BER)? DNA Glycolysase sees the damage and removes it, DNA polymerase puts the tight base back, DNA ligase seals it back up. - correct answer What are the 3 steps in base excision repair? 1 - correct answer How many nucleotides does base excision repair remove? Mismatch Repair (MMR). It is the only one to occur during REPLICATION - DURING THE PROOFREADING - correct answer What is it called when a large section of the nucleotide is removed from the DNA so that DNA polymerase can try again? (This corrects DNA damage) Mismatch Repair (MMR) repairs errors such as G with T instead of G with C. DNA Polymerase fixes it. This happens during replication and MMR removes a large section of the nucleotide from the DNA and DNA Polymerase tries again. - correct answer What repairs a base mismatch? When DNA polymerase takes an individual nucleotide and matches them to the parental sequences to ensure a correct pair. (it must bind with RNA primer to work). ie: DNA Polymerase binds to DNA to make RNA - correct answer What is DNA Transcription? CLEANS damage caused by things such as UV rays and repairs it. A large section of nucleotides are removed, including the damaged portion, along with a few on each side. It is then replaced by DNA polymerase. - correct answer What is NecleoTIDE repair It repairs double stranded breaks (last effort) by copying another strand of DNA and replacing it completely. - correct answer What is Homologous Recombination? Another last effort to repair a double strand break by putting the ends back together before making sure they are correctly copied. This can lead to deletions/insertions (frameshift mutations). - correct answer What is Non-Homologous Recombintaion? It must bind to RNA primer - correct answer What does DNA Polymerase bind to in order to make RNA TRANSCRIPTION DNA take the individual nucleotide and match them to the PARENTAL sequences to ensure a correct pair. introns (non-coding region) are removed and exons (coding region) joined to form a contiguous coding sequence. - correct answer What happens during RNA splicing to generate a mature RNA molecule? The ability to turn genes on and off - correct answer What is Gene Expression? The study of changes in organisms caused by modification of gene expression NOT alternation of the gene code. - correct answer What is epigenetics? Where a DNA molecule wraps around histone proteins to form tight loops called nucleosomes. These nucleosomes coil and stack together to form fibers called chromatin. (genes are ON if the nucleosomes are wide spread and OFF if the genes are tightly packed) - correct answer What is packaging of DNA? Polymerase - correct answer What is needed for DNA replication? A point mutation in a sequence of DNA (change in one nucleotide) that results in a premature STOP codon - correct answer What is NonSense Mutation A mutations in DNA that do not have an observable effect on the organism's phenotype. (1 neucleotide changes but it codes for the same amino acid) - correct answer What is a Silent Mutation? A point mutation in which a single nucleotide change results in a codon that codes for a DIFFERENT amino acid. - correct answer What is a Missense Mutation? It is typically not seen in every generation of an affected family. X-linked dominant disorders are caused by mutations in genes on the X chromosome, one of the two sex chromosomes in each cell. (males and females are equally affected) - correct answer What is Autosomal Dominate? It becomes Ionized Alanine. (Alanine is HYDROPHOBIC and has CH3 as its weak interaction. Ionized means it has a + or -. - correct answer Alanine is an amino acid with an amino group, a carboxyl group, and a methyl group (side chain). What happens if it looses an electron. Amino Acids whose side chains prefer water. (NH, OH, SH) - correct answer What is a Polar Amino Acid? Amino Acids that Can't Have (CH) water (hydrophobic) - correct answer What is a Non Polar Amino Acid? There is a charge (+/-) attached to the amino acid - correct answer What is Ionized Amino Acid? It is caused by tangles inside the cell and plaques outside the cell (senile plaques) caused by abnormal protein aggregation (APA). - correct answer What is the misfolding of protein structure in Alzhiemers disease? It is a fibrous, toxic material inside of cells. When its connections are lost, it becomes defective and forms filaments in the neuron. Its accumulation is triggered by a buildup of Amyloid protein, which disrupts the functioning of brain cells. - correct answer What roll does the protein TAU play in Alzhiemers disease? It is a buildup of excess Amyloid protein between nerve cells. It starts in the hippocampus and moves up, creating senile plaques in the brain. - correct answer How is Amyloid-beta protein linked to Alzhiemers Disease? Protein aggregates usually consist of fibers containing misfolded protein with a β-sheet conformation, termed amyloid. Neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD), amyotrophic lateral sclerosis (ALS) and prion diseases have these protein aggregations. Neurodegeneration and memory loss can be detected before Amyloid fibers accumulate in the brain. - correct answer What is Neurodegenerative protein aggregation? Proteins that bind to denatured proteins and assist in the PROPER folding or unfolding and the assembly or disassembly of molecular structures. (they can help newly formed proteins and help misfolded proteins) - correct answer What is a molecular chaperone? Primary, (formed by peptid bonds) Secondary, (held together by hydrogen bonds, formed from two polar amino acids) Tertiary, (side chain interaction) Quaternary (more than one polypeptide) - correct answer What are the levels of a protein structure? The folding and intramolecular bonding of the linear amino acid chain. Folded proteins are stabilized by thousands of noncovalent bonds between amino acids. THE AMINO ACID SEQUENCE OF A PROTEIN DETERMINES ITS 3D SHAPE. - correct answer What determines the 3D shape of a protein? Folded structures that form within a polypeptide. Stabilized by HYDROGEN BONDS between atoms in the polypeptide backbone. How the chains on amino acids interact with each other to form BETA SHEETS and ALPHA HELIXES. - correct answer What is the Secondary level of protein structure? AcetylCoA starts the citric acid cycle. It produces NADH and FADH2 - correct answer What starts the citric acid cycle and what does it produce? Protein Aggregation - correct answer When this misfolds, it creates a HYDROPHOBIC interaction? Unsaturated - correct answer What type of fat is liquid at room temperature? It allows the cell to continue glycolysis when oxygen is scarce (Anaerobic conditions)...like in skeletal muscles during strenuous exercise. - correct answer What is Fermentation? A chemical reactant that binds with an enzyme to generate a product. - correct answer What is a substrate? lactate produced by anaerobic glycolysis in the muscles moves to the liver and is converted to glucose, which then returns to the muscles and is metabolized - correct answer Where is lactate metabolized? Glycogenesis - correct answer Carbohydrate loading is a strategy used by endurance athletes, such as marathon runners, to maximize the storage of glycogen (or energy) in the muscles. What process does this stimulate? A condition that prevents the body from converting certain fats to energy, particularly during periods without food (fasting). - correct answer What is MCAD Deficiency? (Medium-Chain Acyl-CoA Dehydrogenase) Hyrdogen Bond - correct answer This type of bond is formed from 2 polar amino acids? The protein is heated up and breaks apart. PRIMARY STRUCTURES ARE UNAFFECTED BY DENATURING. - correct answer What happens in Denaturing a Bond? It blocks an enzyme process in cancer cells so that they can not grow. - correct answer How does Methotrexate treat cancer? It is HYDROPHOBIC and can be disrupted by denaturing (heating up) - correct answer What is unique about a tertiary structure? Molecule that is formed when an enzyme comes into perfect contact with its substrate. - correct answer What is a substrate enzyme complex? It serves as the binding platform for a specific substrate and is the site of the chemical reaction. - correct answer What is an Enzymes active site? Any site other than the Enzyme active side where a substrate binds. - correct answer What is an Allosteric site? A molecule SIMILAR to a substrate that can bind to the enzymes active site, but the molecule is unable to react. - correct answer What is an enzymes competitive inhibitor? Molecules that attach to the enzyme in the allosteric site (site other than the active site) - correct answer What is a non-competitive inhibitor? When an end product builds up and binds to an Allosteric site (site other than active site) and stops the pathway. It binds to the enzyme and slows it down. - correct answer What is feedback inhibition? The Tail - correct answer What part of a phospholipid is hydrophobic? They contain carbon bonds and hydrogens (HC, CH2, CH3). They are weak and affected by temperature changes. - correct answer How do you determined a non-polar amino acid? Alzheimer's - correct answer What disease is protein aggregation associated with? AUTOSOMAL RECESSIVE pattern, which means that both copies of the gene in each cell have mutations . The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition. - correct answer What type of inheritance is sickle cell anemia? The RNA in a sickle hemoglobin changes from GAG to GUG - correct answer What happens to hemoglobin in sickle cell? oxygen binding increases the affinity of hemoglobin for more oxygen. (when one molecule of O2 leaves, the other 3 leave...when one hgb picks of O2, the others pick up O2). So, O2 will bind quicker when there is another O2 molecule already there (Bohr) - correct answer What is Cooperative Binding? Carbon Monoxide binds stroner than O2. Carbon Monoxide picks up O2 but doesn't drop it off. - correct answer Describe Carbon monoxide Poisoning. Her affinity (stickiness) for oxygen is lower, so the mother becomes deoxygenated and the fetus has a higher affinity to get it from its mother. - correct answer What does it mean if a mothers 2, 3 BPG is higher than her fetus? The structure is tense, heme is DOMED SHAPE and Ph is lower. (LOW Ph in tissue and muscles) - correct answer What happens to the structure of hemoglobin in the absence of oxygen? Hemoglobin has a low affinity for Oxygen and transports it. Myglobin has a high affinity for oxygen and stores it (not affected by Ph) - correct answer What is the difference in the affinity (stickiness) of Hemoglobin and Myoglobin? Higher Ph/low CO2, or Left shift, increases the affinity (stickiness) for Oxygen and Lower Ph/high CO2, or Right shift, decreases the affinity for Oxygen. (Hemoglobin is saturated sooner and reaches 100% earlier with a left shift) - correct answer How does Ph influence O2 saturation of Hgb at the same partial pressure? High Cholesterol - correct answer What makes LDL? Myoglobolin is contained in the muscle, but released into the blood stream if muscle is damaged (Troponins) - correct answer What protein can show an Myocardial Infarction? It requires energy to synthesize larger molecules (ends in -GENESIS) This is where there is no O2 - correct answer What is an Anabolic Pathway? Generates energy by breaking down larger molecules (ends in -LYSIS) - correct answer What is a Catabolic Pathway? Glucose (in the liver, gluconeogenesis converts 2 molecules of lactate into glucose) - correct answer What does the Cori Cycle supply for Red Blood Cells? Acytle CoA - correct answer What molecule starts the citric acid cycle? To continue with aerobic metabolism - correct answer Why are NADH and FADH2 needed in the Citric Acid Cycle? The formation of Glycogen from sugar - correct answer What is Glycogenesis? Glucagon stimulates breakdown of glycogen stored in the liver, stimulating an increase in blood concentration of glucose. - correct answer How does glucagon affect carbohydrate metabolism? It is the only way to make ATP without Oxygen present - correct answer What is substrate level phosphorylation? Is an Insulin regulated glucose transporter that allows glucose into the cell. (found in skeletal muscle and fat tissue) - correct answer What is GluT4? It inhibits liver glucose output by using Gluconeolysis and Gluconeogenesis. - correct answer How does Metformin work? Stimulates glycogenolysis to release glucose for the liver to export to the blood stream. (active when blood sugar is low). It releases glucose from storage (glycogen) to increase blood sugar. - correct answer What is Glucagon? Gluco (Gulcose) Neo (new) Genesis (make). Turns amino acids into glucose) - correct answer What is Gluconeogenesis? Gluco (Glucose) Genesis (make). Happens in liver or muscle) - correct answer What is Glucogenesis? Glcyo (Glucose) Lysis (break) The breakdown of glucose by enzymes, releasing energy and pyruvic acid. - correct answer What is Glygolysis? The irreversible binding of glucose with proteins and lipids. (contributes to atherosclerosis) - correct answer What is Glycation? A 6 carbon sugar that fuels our tissues - correct answer What is Glucose? A storage form of Glucose that stores carbohydrates - correct answer What is Glycogen? Breaks down glycogen to release glucose (caused by fasting) - correct answer What is Glycogenolysis? Tap into their glycogen stores and stimulate glycolysis - correct answer If a person is running and loosing, what do they need to do? In the Mitochondria (occurs in a fasting state) - correct answer Where does Beta Oxidation occur? Where fatty acids are broken down and CoA is added to make fatty Acyl CoA - correct answer What is Beta Oxidation? ATP, NADH, FADH2 - correct answer What molecules are produced by Beta Oxidation? Seven ( # 6 count Carbons/2) and Six (answer -1_) - correct answer Beta Oxidation of C18 fatty acid will make _______ Acetyl Coa units after _______ rounds of beta oxidation? The body cannot fully break down fat to release energy quickly. So avoid long periods of fasting. Eat complex carbs and avoid fats. - correct answer What diet should a pt with MCADD be on? Between the sixth and seventh carbons. (Omega 3 is between the thrid and fourth carbons) - correct answer Where is the first double bound on an Omega 6 fatty acid? Liquid at room temp, don't stack well, Lower melting point (olive oil) - correct answer What are the characteristics of Unsaturated bonds? Mitochondrail matrix - correct answer Where are fatty acids catabolized? Fatty acid synthesis begins with acetyl CoA, which must first be transported to the CYTPLASM. In the CYTOSOL, a series of steps link the carbons from acetyl CoA molecules into a new fatty acid chain. - correct answer Which of the following accurately describes the steps involved in fatty acid synthesis? (where does it occur) When both hydrogens are on the same side of the double bond.. It takes less heat to melt (because it is not packed tightly), it forces a kink in the carbon chain. - correct answer What is CIS configuration? When the hydrogen is on opposite sides of the double bond. It takes more heat to melt (because they are packed tightly). - correct answer What is TRANS configuration? tryglicerides (a person wanting to limit fats) - correct answer This is a picture of the greatest reserve of energy (Glycerol backbone with 3 fatty acid chains) Compound that comes from Polyunsaturated Fatty Acid. It aids with inflammation, fever, immunity, and blood coagulation. THEY ARE SIGNALING MOLECULES - correct answer What is an Eicosanoid? Where Fatty Acids and Triglycerides have a leaky membrane and Phospholipids are packed tight. The tails are hydrophobic and the polar heads are hydopholic (like water). - correct answer What is the Fluid Mosaic Model? 2 - correct answer How many fatty acid tails do Phospholipids have? One parent has type A, and the other parent has type B; one parent has type A or B and the other parent has type AB; Both parents have type AB. - correct answer If a child has AB blood, what blood type is it's parents? Hgb carries oxygen in its relaxed state and has a higher affinity (more stickiness). - correct answer What are the characteristics of Hemoglobin in its R (relaxed) state, as opposed to its T (tense) state. Mainly in the liver and muscle tissues - correct answer Where is glycogen stored? Glycogen stores Glucose in the liver when there is excess. Then it can be broken down back to Glucose to be released into the muscle tissue. - correct answer What is the difference in function of Glucose and Glycogen? Cori Cycle - correct answer Which process is an example of anaerobic metabolism and uses Glycolysis, Lactate Fermentation, and Gluconeogenesis (GLG) Gluconeogenesis - correct answer What converts pyruvate into oxygen? Glycolysis will stop - correct answer What will happen if NAD+ is too low? It has hexagons and pentagons - correct answer How do you identify a Cholesterol Fatty Acid Chain? Shaped like a Bobby pin - correct answer How do you identify a eicosanoid fatty acid? Double Bond(s) - correct answer How do you identify an unsaturated fatty acid chain? It has 8-12 carbons - correct answer How do you identify a medium chain fatty acid? EACH parent has a dominate gene and a recessive gene (Xx and Xy) - correct answer What is heterozygous? EACH parent 2 of the same gene (XX or xx) - correct answer What is homozygous? Hydrogen - correct answer What determines the structure of secondary protein? Peptide composer of two amino acids - correct answer What is a dipeptide? NADH to NAD+ - correct answer What does pyruvate recycle in fermentation? Mitochondria - correct answer Where are fatty acids catabolized? Chaperones - correct answer What helps denatured proteins in folding? An increase in NAD+ - correct answer What stimulates beta oxidation of fatty acids? Acetone is produced in the blood - correct answer What happens with a low carb high fat diet? Maintains membrane fluidity - correct answer What role does cholesterol play in the cell Triglycerides, ketones, fatty acids - correct answer What is used for ATP when sugar isn't present? X-linked dominant - correct answer A father with only daughters affected (anywhere in the tree) Changing the 3 dimensional shape - correct answer How does increasing temperature inactivate enzymes? feedback inhibition - correct answer Reversible, non competitive inhibition (control catalytic activity) When a drug binds to a allosteric site and changes the structure - correct answer Non competitive inhibition Carbon dioxide decreases - correct answer What happens to tissue when oxygen saturated hemoglobin increases? Carbon dioxide increases and oxygen decreases. (an increase in CO2 results in a decrease in blood pH, resulting in hemoglobin proteins releasing their load of oxygen. Conversely, a decrease in carbon dioxide provokes an increase in pH, which results in hemoglobin picking up more oxygen) - correct answer What happens to carbon dioxide and oxygen when pH decreases? True (Increased affinity is caused by a conformational change, or a structural change in the hemoglobin molecule) - correct answer T or F the binding of oxygen to a gene changes the structure? Monosaccharides attaches to a lipid - correct answer Glycolipid Ketones - correct answer ____________ decreases when glycagon is released in the blood It's the final electron acceptor in the electron transport chain - correct answer What is oxygens role in aerobic metabolism? amino acids - correct answer What molecule is used in gluconeogenesis? It STIMULATES the uptake of glucose from the blood - correct answer How does insulin impact carbohydrate metabolism? Missfolding protiens - correct answer What causes plaque formation? When pH is low Carbon is high, Hydrogen is high, Acidic, Right shift, Tense state. - correct answer What does CHART stand for Primary - correct answer PROTEIN and AMINO ACID disruption affects which structure?
Escuela, estudio y materia
- Institución
- Biochemistry
- Grado
- Biochemistry
Información del documento
- Subido en
- 2 de agosto de 2023
- Número de páginas
- 15
- Escrito en
- 2023/2024
- Tipo
- Examen
- Contiene
- Preguntas y respuestas
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