100% satisfaction guarantee Immediately available after payment Both online and in PDF No strings attached 4.2 TrustPilot
logo-home
Exam (elaborations)

WGU C785 Final Exam Questions and Answers Latest 2022/2023,100% CORRECT

Rating
-
Sold
-
Pages
33
Grade
A+
Uploaded on
06-04-2023
Written in
2022/2023

WGU C785 Final Exam Questions and Answers Latest 2022/2023 What is the basic structure of an amino acid? What do they look like? - correct answer amino group (NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C), and variable group How do you identify the 3 different types of side chains: non-polar/hydrophobic, polar, and charged? - correct answer Non-polar/hydrophobic - end with CH or "can't have" water. Polar - end with OH, SH, or NH. Charged - end with a charge what kinds of bonds do each of the 3 different types of side chains make? - correct answer ionic, hydrophobic/non-polar, charged What are the 4 levels of protein structure? - correct answer Primary - linear structure, Secondary - Folded into helix or pleated sheet caused by hydrogen bonding, tertiary - 3D structure caused by side chain interactions, quaternary - 1+ amino acid chains combine = multiple subunits MUST have 1+ subunit What enviormental change breaks each type of bond? - correct answer hydrophobic - temperature change, ionic - salt or decreased pH, hydrogen - temperature, change in pH, disulfide - reducing agents what type of amino acid side chain leads to protein aggregration? - correct answer hydrophobic bonds how do environmental changes affect protein folding? - correct answer Extreme temp can cause hydrogen bonds to break apart = malformation of protein folding how do mutations affect protein structure? - correct answer Can cause structure to change. Protein loses form = loses function. May form a different protein. What is an electron? - correct answer Negatively charged atom on outer ring for bonding What is energy: - correct answer Power derived fro chemical interaction what are covalent bonds? - correct answer chemical bond, atoms share 1+ valence electrons what is an ionic bond? - correct answer bond between positive and negative what is a hydrogen bond? - correct answer weak bond between positive and negative with an amino? - correct answer piece of amino acid, NH2 or NH3 what is a carboyxl? - correct answer piece of amino acid, COO or COOH What is hydrophobic? - correct answer Doesn't like water, end with CH what is hydrophilic? - correct answer Water loving, end with OH, NH, or SH what is disulfide bond? - correct answer strongest bond between reduction agents, formed between SH's. what are zwitterions? - correct answer amino with positive and negative charges = overall charge of zero what is a polypeptide - correct answer polymer of amino acids What is dehydration synthesis? - correct answer Process of forming peptide bonds what is hydrolysis? - correct answer adding water to destroy bonds what is an alpha helix? - correct answer twisted secondary structure, formed by hydrogen bonds what is a beta sheet? - correct answer folded second structure shape, formed by hydrogen bonds what is denaturation? - correct answer loss of shape duet o interruption of chemical bonds; occurs via extreme salt, temp, pH what is aggregation? - correct answer clumping of inner or outer cellular proteins caused by misfolded proteins leading to diseases such as Alzheimers, ALS, Parkinson's how do enzymes catalyze reactions? - correct answer bind with substrates to decrease activation energy required and decrease reaction rate how do enzymes affect reaction rate and activation energy? - correct answer decrease activation energy and decrease reaction rate what are the 4 steps of the enzymatic cycle? - correct answer enzyme recognizes substrate, substrate attracts the enzyme; enzyme-substrate complex is formed; enzyme-product complex formed; product is released, enzyme recycled how do environmental changes affect enzymes? - correct answer High heat, pH change, high salt concentration, and reducing agents can cause an enzyme to lose its form/lose function what is a competitive inhibitor? - correct answer Mimics substrate and takes its place on the active binding site what is a noncompetitive inhibitor? - correct answer Binds to allosteric site causing active site to change shape = preventing substrate from binding with enzyme what molecules increase/build up or decrease given a specific inhibitor? A -> (enzyme 1) -> B -> (enzyme 2) -> C -> (enzyme 3) -> D. Pretend Enzyme 2 is inhibited. - correct answer Inhibitor would cause a build up for product B, decrease product C. Enzyme 3 and product D would not be created. what is substrate? - correct answer the substance on which an enzyme acts what is a product? - correct answer result of a reaction what is an intermediate? - correct answer products produced in an enzyme pathway before final product what is an active site? - correct answer location where substrate binds with enzyme what is enzyme specificity? - correct answer Enzymes bind with certain substrate or type of substrate to create a certain reaction what is induced fit? - correct answer Enzyme changes shape in enzyme-substrate complex to facilitate formation of enzyme-product complex what is kinase? - correct answer Enzyme, adds phosphate group via phosphorlation what is phosphatase? - correct answer enzyme, removes phosphate group via dephosphorylation with is an allosteric site? - correct answer secondary site on an enzyme an inhibitor binds to via non-competitive inhibition what is competitive inhibition? - correct answer enzyme substrate and inhibitor complex compete to bind with enzyme's active site. no product formed when inhibitor binds with enzyme. what is non-competitive inhibition? - correct answer inhibitor binds to allosteric site, not active site. Changes shape of active site, preventing substrate from binding and making product what is feedback inhibition? - correct answer End product sends feedback to beginning of enzyme pathway inhibiting 1st enzyme via noncompetitive inhibition what nucleotides/bases are used in DNA? what are their abbreviations/full names? - correct answer C - cytosine, G - guanine, A - adenine, T - thyamine what nucleotides/bases are used in RNA? - correct answer C - cytosine, G - guanine, U - uracil, A - adenine which nucleotides base-pair together in DNA? - correct answer T-A, G-C which nucleotides base-pair together in RNA? - correct answer U-A, G-C how to we make complementary DNA? (i.e. coding to temple et reverse) - correct answer Taking coding DNA, write in reverse, then pair them up to make template. Template DNA, write in reverse, then pair up to make coding how do we make mRNA? - correct answer template DNA to mRNA by switching back and forth OR coding DNA to mRNA by switching out T's for U's which strand of DNA is complementary to mRNA? - correct answer Template DNA how do we make protein? - correct answer DNA -> RNA -> Protein which type of nucleotide sequence is used and in which direction? - correct answer RNA is used 5' to 3' what is the relationship between mRNA and tRNA? - correct answer tRNA is complementary to mRNA how does mRNA splicing allow use to create multiple proteins from a single gene/mRNA? - correct answer Alternative splicing allows for all introns to be cut and some exons = multiple proteins form from same MRNA what factors increase gene expression? - correct answer Decreased methylation, increased acetylation, Widely spaced neucleosomes, exposed promoter, use of transcription factors, use RNA polymerase what factors decrease gene expression? - correct answer Increased methylation/decreased acetylation, tightly packed nucleosomes, hidden promoter, no transcription factors, no RNA polymerase what steps do you take to determine what type of mutation occurred between a normal and mutated DNA/RNA sequence? - correct answer look between the two strands, determine what changed, name the mutation What are the types of mutations? - correct answer silent, missense, nonsense, frameshift what type of DNA damage does each repair pathway fix? - correct answer base excision - single nucleotide, nucleotide excision repair - multiple nucleotides, missmatch - mistakes made in DNA replication, homologous recombination/nonhomologous end joining - double stranded breaks what are the steps of excision repair? - correct answer Recognize damage, cut damage out, recreate DNA strand, glue DNA strand back together what are the steps of mismatch repair? - correct answer Remove mismatched base, try again what are the steps of homologous recombination and nonhomologous end joining? - correct answer HR uses DNA from unbroken strand to fix broken strand, NHEJ reconnects broken pieces, may have pieces missing what are the steps of PCR? - correct answer denature, anneal, elongation/extension how do we denature DNA in PCR? - correct answer heat to 95 degrees C to separate DNA strands how do we anneal DNA? - correct answer primers base pair with DNA strands how do we elongation/extend DNA? - correct answer DNA polymerase attach primers and synthesize new DNA strands what are the components of PCR? - correct answer target DNA, heat stable DNA polymerase, nucelotides (dNTP), primers how are primers used to assist in a PCR reaction? - correct answer Primers allow DNA polymerase to bind to target DNA how do you calculate the number of copies of DNA produced by specific number of PCR cycles? - correct answer Each cycle produces doubles the amount of DNA how does PCR compare to normal DNA replication in the cell? - correct answer RNA primers used instead of DNA in normal replication. Helicase enzymes separate DNA strands instead of heat in normal replication. DNA polymerase is not heat stable in normal replication. what is gene expression? - correct answer process by which info coded in DNA creates proteins and RNAs What are nucleotides? - correct answer building blocks of nucleic acids what is antiparallel? - correct answer refers to arrangement of DNA double helix (run in opposite directions) what is complementary? - correct answer predictable counterparts what is template DNA? - correct answer DNA strand, provides pattern for ordering via complementary base pairing in RNA transcript what is coding DNA? - correct answer nontemplate strand of DNA, same sequence as mRNA except has T instead of U what is replication? - correct answer processing of copying DNA molecules via DNA synthesis what is transcription? - correct answer creation of RNA using info from DNA What is RNA polymerase? - correct answer enzyme, links ribonucleotides to growing RNA chain during transcription what is a promoter? - correct answer sequence of DNA that binds with RNA, encourages RNA transcription what is a transcription factor? - correct answer proteins that bind to promoter regions, help initiate transcription what is mRNA? - correct answer type of RNA, created via DNA template, specifies primary structure of protein what is translation? - correct answer creation of polypeptide using info in the mRNA what is tRNA? - correct answer RNA that brings amino acids to ribosomes during creation of polypeptide what are ribosomes? - correct answer molecular complex, assist with orderly linking of amino acids/polypeptide chains what are codons? - correct answer nucleotide triplet of DNA or RNA. Basic genetic code. Specifies type of amino acid or termination signal what are anticodons? - correct answer nucleotide triplet at one end of tRNA. Base pairs with complementary codon on mRNA what is splicing? - correct answer parts of transcript are removed and others are reconncected what are introns? - correct answer pieces of noncoding that are removed during RNA processing what are exons? - correct answer pieces of coding that stay with RNA during processing - ARE NOT DISCARDED what are histones? - correct answer Protein; high proportion and charged amino acid that binds with DNA. Plays key role in chromatin structure. what is a nucleosome? - correct answer basic bead like unit of DNA. what is methylation? - correct answer presence of methyl groups on DNA bases, adding of methyl groups to DNA bases what is acetylation? - correct answer attachment of acetyl groups to certain amino acids of proteins (mainly histones) what is the structural difference between myoglobin and hemoglobin? - correct answer myoglobin - primary, secondary, tertiary, single subunit protein (1 heme, 1 iron, 1 O2). hemoglobin - primary, secondary, teriary, quaternary, 4 subunit protein (4 heme, 4 iron, 4 O2) what are the functional differences between myoglobin and hemoglobin? - correct answer myoglobin - found in muscle, stores O2 in muscle, higher affinity for O2. hemoglobin - found in blood, delivers O2 to tissues in need, decreased affinity for O2 what are the structural properties of the tense state of hemoglobin? - correct answer deoxygenated hemoglobin = deep purple color. heme is bent; subunits move farther apart. decreased affinity of O2 binding. what is the structural properties of hemoglobin in the relaxed state? - correct answer Bright red color. Heme is planar with subunits moved closer, increased affinity of O2 binding what causes hemoglobin to change between relaxed and tense state? - correct answer O2 binding with hemoglobin in tense state causing subunits to move in closer and change hemoglobin to relaxed state how does carbon monoxide affect the structure of hemoglobin? - correct answer locks HgB in R-state, and takes up space on HgB for binding to O2 how does it cause carbon monoxide poisoning? - correct answer keeps HgB in R- state, HgB does not release O2. HgB has higher affinity for O2, but CO has higher affinity than HgB for O2. steps of DNA replication to protein? - correct answer DNA -> transcribed -> mRNA - > translation -> protein what is an okazaki fragment? - correct answer Okazaki fragments are short molecules of single-stranded DNA that are formed on the lagging strand during DNA replication. how does 2,3-BPG (2,3-DPG) affect structure of hemoglobin? - correct answer reduces hemoglobin's affinity for O2 what is the natural function of 2,3-BPG? - correct answer increases release of O2 in atmosphere with decreased oxygen. efficiently deliver oxygen to fetus. what are we measuring when we measure pH? - correct answer number of H+ protons in blood what level of pH is blood considered acidic? - correct answer Below 7.2 what level of pH is blood considered basic? - correct answer above 7.4 what factors change pH in blood? - correct answer Increased or decreased CO2, increased or decreased H+ how to do changes in pH affect hemoglobin's structure? - correct answer Increased CO2/Increased pH = T-state, Decreased CO2/Decreased pH = R-state what is a heme? - correct answer subunit of hemoglobin/myoglobin what is affinity - correct answer stickiness of oxygen binding what is cooperativity? - correct answer binding of O2 to deoxygenated blood what is bicarbonate? - correct answer carbon dioxide in disguise, outcome of CO2/H2O + carbonic anhydrase what is carbonic anhydrase? - correct answer enzyme; converts CO2 into bicarb and proton what do chaperones do? - correct answer assist with protein folding difference between fetal and adult hemoglobin? - correct answer fetal hemoglobin has higher affinity for oxygen than maternal hemoglobin. fetal has alpha and gamma forms of hemoglobin while adults have alpha and beta Right left shift curve for decreased pH? increased pH? - correct answer Decreased pH = right shift curve. Increased pH = left shift curve. what can show an MI? - correct answer myoglobin - can show muscle damage Examples of monosaccharides - correct answer glucose, fructose, galactose examples of disaccharides - correct answer sucrose, lactose, maltose examples of polysaccharides - correct answer starch, glycogen, cellulose, chitin how do the different linkages between monomers of polysaccharrides affect how they are digested? - correct answer B linkages - enzymes that break down B linkages, unable to break down A linkages. A linkages - enzymes only able to break down A linkages. structure and function of ATP? - correct answer 3 phosphate groups + adenosine. provide energy to cell real-life scenarios that would like to insulin release from pancreas? - correct answer eating carb rich meal, eating something excessively sugary how does insulin help reduce blood sugar level? - correct answer promote glycogen formation from excess glucose, stimulates glucose uptake by cells how does glut4 aid in this process? - correct answer protein channels open in presence of insulin, allow glucose to pass from bloodstream to cell what are some real life scenarios that would lead to glucagon release from the pancreas? - correct answer blood glucose level getting too low due to fasting how can diabetes lead to glycation and AGEs? - correct answer diabetes is insulin resistance or lack of insulin production = increased blood sugar. glucose links with proteins when there is too much. glycated collagen has decreased elasticity of veins = damage to capillaries, eyes, kidneys, nerves What is catabolism? - correct answer breaking down molecules what is anabolism? - correct answer building up what is a carbohydrate? - correct answer macromolecule. a type of sugar. What is a monosaccharide? - correct answer single sugar What is a disaccharide? - correct answer double sugar What is a polysaccharide? - correct answer macromolecule; made from hundreds to thounsands of monosaccharides. stores as glycogen and startch. what are alpha linkages? - correct answer seen in animal polysaccharides. look the same in linkages. what is a beta linkage? - correct answer seen in plant polysaccharides. face in opposite directions. what is insulin? - correct answer hormone; lowers blood sugar what is glucagon? - correct answer hormone; raises blood sugar what is glycogen? - correct answer form of glucose storage in liver What is glycogenesis? - correct answer formation of glycogen from glucose what is glut4? - correct answer glucose transporter what is glycogenolysis? - correct answer glycogen breakdown, release of glucose what is aerobic metabolism? - correct answer ATP production using oxygen, breaks down fats and carbs. what is cellular respiratoin? - correct answer cathbolic pathways of aerobic and anaerboic; break down molecules by using electron trainsport chain for ATP production what is glycolysis? - correct answer breakdown of glucose, creates 2 new ATP and 2 pyruvate What is the citric acid cycle? - correct answer creation of 3 NADH and 1 FADH2 and 2 CO2 molecules in each turn of the cycle what is ETC? - correct answer electron transport chain; accepts electrons from FADH2 and NADH, uses their energy to pump protons to intermember space what does NAD/NADH do? - correct answer transports electrons of the highest energy to and from complex 1 what does FAD/FADH2 do? - correct answer transports electrons to/from complex 2 What is substrate level phosphorylation? - correct answer ATP synthesis by direct transfer of phosphate group to ADP from an intermediate substrate What is oxidative phosphorylation? - correct answer production of ATP using energy derived from ETC reactions; 3rd stage of cellular respiration what is anaerboic metabolism? - correct answer atp production without oxygen what is fermentation? - correct answer catabolic process; makes limited amounts of atp without ETC, produces lactic acid or eythl alcohol what is gluconeogensis? - correct answer formation of glucose from non- carbohydrate sources what is the cori cycle? - correct answer fermentation + gluconeogenesis, way to make 2 ATP in muscle what is metformin? - correct answer diabetic medication for Type 2 DM. Decreased gluceoneogensis in liver/increases glucose uptake by muscle what is glycation? - correct answer colvalent bond of a sugar to a protein What are advanced glycation end products (AGEs)? - correct answer sugars bonded with proteins; effects collagen by decreasing elasticity of blood vessels = damage to nerves, kidneys, and eyes what are the roles of NADH and FADH2? - correct answer transport electrons from CAC to ETC how is NADH generated in glycolysis? - correct answer glycolysis consumes 2 NAD to create 2 NADH how are NADH and FADH2 generated in the citric acid cycle? - correct answer each turn of CAC creates 3 NADH molecules and 1 FADH2 how does the ETC use NADH and FADH2? - correct answer NADH and FADH2 bring high energy electrons to complex 1 and 2; ETC uses their energy to power the proton pump which complexes accept NAHD and FADH2? - correct answer NADH -> complex 1, FADH2 -> complex 2 what is the role of the electrons in the ETC? - correct answer provide energy to pump protons from mitochondrinal space to intermembrane space what is the role of protons in atp product? - correct answer protons provide energy to make atp as they cross the inner membrane what enyme ultimately makes atp? - correct answer atp synthase what is the role of oxygen in the ETC? - correct answer oxygen binds with exhausted electrons from complex 4 to create water how do fats and proteins enter aerobic metabolism? - correct answer proteins -> amino acids -> pyruvate or acteyl CoA or CAC. fats -> fatty acids -> acetyl CoA what are the two different fates of pyruvate? - correct answer pyruvate can be convereted to ethyl alcohol or lactic acid in fermenttaion or acetyl CoA in aerobic metabolism what factors affect the use of pyruvate by the cell? - correct answer presence of oxygen in the catabolism how are aerobic and anaerobic metabolism the same? - correct answer both use glucose, both create ATP and CO2, both use glycolysis in the cytoplasm how are anaerobic and aerobic metabolism the different? - correct answer aerobic metabolism utilizes oxygen and can produce more ATP (36). Anaerobic metabolism does not use oxygen and creates 2 ATP which aeroboic and anaerobic pathways are controlled by insulin? - correct answer Insulin inhibits: gluconeogensis, glycogenolysis Insulin promotes: Glycolysis, glycogenesis which aerobic and anarobic pathways are controlled by glucagon? - correct answer Glugcagon promtes: gluconeogensis, glycogenolysis Glucagon inhibits: glycolysis, glycogensis what are the differences between type 1 and types 2 diabetes? - correct answer Type 1 is an autoimmune disorder effeting beta cells in pancreas, unable to produce insulin. Type 2 is when target cells are not responding to insulin; insulin is produced, but cells aren't receptive/glucose remains elevated how does metformin treat diabetes? - correct answer decreases glucogenesis in the liver and increases glucose uptake by the muscle cells how does metformin relate to glut4 and gluconeogensis? - correct answer glut4 enables glucose to pass from blood to cell in presence of insulin. metformin increases presence of glut4 or makes it more responsive; decreases gluconeogensis in liver. how does length of a fatty acid affect its melting point and physical state at room temp? - correct answer shorter the fatty acid = lower melting point, liquid at room temp. longer the fatty acid = higher melting point, solid at room temp how do we label the different carbons and bonds in fatty acid? - correct answer alpha, beta, or omega carbons/bonds and single or double bonds. *alpha bond links with carboxyl group, beta joins alpha and beta together* how do we count the carbons in a full structure of a fatty acid? - correct answer from the omega end how do we count carbons in a structure formula? - correct answer start at end, work your way with smalle groups to write mathematical equation counting carbons in a zig-zag struture? - correct answer more simplified; carbons at the points (or bends) of zig-zag structure what are the structural differences between saturated and unsaturated fats? - correct answer saturated fats do not have double bonds between carbons while unsaturated fats do how does affect melting point and physical state at room temp of unsaturated/saturated fats? - correct answer saturated fats are mostly solid at room temp while unsaturated fats are mostly liquid at room temp how can I recognize structure of triglycerides, cholesterol, and phospholipids? - correct answer triglycerides - 3 fatty acid chains and 1 glycerol. phospholipids - 2 fatty acid tails and 1 phosphate head. cholesterol - 4 member ring Functions of cholesterol, phospholipid, and triglycerides? - correct answer cholesterol - membrane buffer/maintain integrity of membrane. phospholipid - major component of cell membrane. triglyceride - ATP storage how do we break down a triglyceride? - correct answer digested by stomach and small intestine by enzumes such as lipases by using hydrolysis where in the cell does fatty acid breakdown occur? - correct answer matrix of mitochondria what happens to the different components of the triglyceride? - correct answer broken into glycerol and fatty acids. picked up by epithelial cells. how do we break down a fatty acid? - correct answer beta oxidation where in the cell does beta oxidation take place? - correct answer Fatt acetyl CoA molecules enter mitochondrial matrix and begin beta oxidation cycle what are the 3 products of beta oxidation? - correct answer 1 acetylCoA, 1 NADH, 1 FADH2 how do we calculate the number of acetylCoA produced from a fatty acid? - correct answer number of carbons in a fatty acid divided by 2 how do we calculate the number of rounds it takes to break it down completely? - correct answer one less than the number of acetylCoA moleules produced how do we calculate the amount fo ATP produced? - correct answer number of acetylCoA molecules mulitplied by 14 what happens to the products of beta oxidation after they are produced? - correct answer enter ETC for further ATP production how and why are ketone bodies produced? - correct answer produced by breaking down fatty acids in liver cell's mitochondria; produced when body has decreased carbs or increased fatty acids for energy needs. Ketones make 22 ATP each. **alternative energy form** ***Seen with Type 1 DM, starvation, alcoholism*** what is the molecule use for fatty acid synthesis? - correct answer acetyl-COA how is acetyl-COA exported from the mitochondria to the cytosol? - correct answer must pair with oxaloacetate to make citrate, cross into cystol, break apart to become acetylCOA again what is the comitted step of fatty acid synthesis? - correct answer formation of malonyl COA by acteyl COA carboxylase **needs citrate and CO2** which fatty acid metabolism pathways are controlled by insulin? - correct answer Insulin encourages lipogensis which fatty acid metabolism pathways are controlled by glucagon? - correct answer glucagon encourages lipolysis what are the components of the plasma membrane? - correct answer phospholipids how do cells maintain fluidity of the plasma membrane when moved to colder or warmer temperatures? - correct answer ratio of saturated/unsaturated fatty acids acting as buffer what does it mean for a nutrient to be essential? - correct answer must come from the diet what are the 3 pathways of anerobic metabolism? - correct answer glycolysis, fermentation, gluconeogensis where in the cell does each pathway take place? - correct answer Glycolysis - cytoplasm, Fermentation - cytoplasm, Gluconeogensis - liver what are the products of each anaerobic pathway? - correct answer glycolysis - 2 ATP, 2 NADH, 2 H; fermentation - 2 lactate, 2 NAD; gluconeogensis - 1 glucose whatis the role of fermentation in regards to NAD/NADH? - correct answer fermentation utilized by cells to regenerate NAD what are at least 3 different molecules that can be used as substrates of gluconeogensis? - correct answer lactate, acteyl COA, glycerol, aminoacids how much atp is used in gluconeogensis? - correct answer 6 ATP is used what is the net outcome of atp in the cori cycle? - correct answer Net loss of 4 ATP how does glucagon help increase blood glucose? - correct answer glucagon promotes release of glucose from energy stores such as liver's glycogen what are the 3 pathways of aerobic metabolism? - correct answer glycolysis, citric acid cycle, electron transport chain + oxidative phosphorylation where in the cell do the aerobic pathways take place? - correct answer glycolysis - cytoplasm, citric acid cyle - mitochondrial matix, oxidative phosphorylation/ETC - mitochondrinal inner membrane what molecules are the "ins" of each aerobic pathway? - correct answer Glycolysis - glucose, 2 ATP, 2 NAD, 4 ADP. CAC - acetylCOA, NAD, FADh, H+. ETC - NADH, FADH2 what molecules are the products of the aerobic pathways? - correct answer glycolysis - 2 pyruvate, 4 ATP, 2 NADH, 2 ADP; CAC - NADH, CO2, FADH2, ATP; ETC - NAD, FAD, ATP how do the products of the aerobic pathways become substrates for the next pathways? - correct answer pyruvate from glycolysis turn into AcetylCOA during pyruvate oxidation. Acetyle COA enters CAC producing "carrier" NADH and FADH2 that enter the ETC how is atp generated in glycolysis? - correct answer breaks on 6 carbon glucose into 2 3-carbon pyruvates and produces net total of 2 new ATP how is ATP generated in the ETC? - correct answer uses energy from the electrons to pump protons and create proton gradient - the energy source for ATP synthase to make ATP how many ATP are generated in each aerobic pathway? - correct answer glycolysis - 2 ATP, CAC - 2 ATP, ETC - 26 to 28 ATP What are the fat soluble vitamins? - correct answer A, D, E, K what are the two essential fatty acids and how do we recognize that a fatty acid is essential? - correct answer omega 3 and omega 6 fatty acids. by looking to see where the double carbon is. how can you recognize the structure of a eicosanoid? - correct answer arachidonric acid - 20 carbon fatty acid, omega 6 fatty acid. Looks like incomplete oblong circle in zig-zag formation what are the functions of eicosanoid? - correct answer inflammation, pain, fever, blood pressure, blood clotting, and reproduction how is the function of eicosanoid affected by aspirin? - correct answer ASA targets eicosanoid production, specifically cox enzymes. decrease prostaglandin production of pain and inflammation what is a saturated fatty acid? - correct answer fatty acid without double bonds within hydrocarbon chain what is an unsaturated fatty acid? - correct answer fatty acid with one or more double bonds within hydrocarbon chain What is a triglyceride? - correct answer a lipid made of one glycerol and three fatty acids what is cholesterol? - correct answer a steroid; found in animal membranes. has a tetracyclic ring, acts as buffer. what is a phospholipid? - correct answer similiar to triglycerides; has two fatty acids and one phosphate. love and hates H20 what is a micelle? - correct answer spherical single layer of phospholipids; transport fatty acids, vitamins, and cholesterol what is an adipocytes? - correct answer fat cells what is lipase? - correct answer enzyme that catalyzes triglyceride breakdown what is lipolysis? - correct answer breakdown of lipids what is beta oxidation? - correct answer fatty acid breakdown in mitochondria to 1 acetyle COA, 1 NADH, and 1 FADH2 what are ketone bodies? - correct answer alternative energy form; comes from fatty acid breakdown what is ketoacidosis? - correct answer accumulation of too many ketones within the body what is MCADD? - correct answer defect in enzyme used for beta oxidation; need to avoid fasting, eat slow release carbs what is fatty acid synthesis? - correct answer linking of acetylCOA repeatedly to make new fatty acids in the cytoplasm what is oxaloacetate? - correct answer Intermediate that couples with acetyl Co-A to form citrate what is citrate? - correct answer Bridge between carb and fatty acid metabolism; important for fatty acid synthesis what is amphipathic? - correct answer molecules that are hydrophilic and hydrophobic what is the phospholipid bilayer? - correct answer polar heads interact with watery environment; nonpolar tails remain inside to avoid water. controls in/out of cell. what is the plasma membrane? - correct answer boundary of every cell, acts as selective barrier, regulates chemical composition what is a glycolipid? - correct answer lipid + sugar; bases for A, B, and O blood types what is a glycoprotein? - correct answer sugar + protein; basis for A, B, and O blood types what is an essential fatty acid? - correct answer omega 3 and omega 6 fatty acids, must be eat thru diet what is an eicosanoid? - correct answer class of lipids derived from essential fatty acids; act as local hormones generated as needed; control fever/pain/BP/reproduction/blood coagulation what is an arachidonic acid? - correct answer precursor to ecosanoids what is chylomicron? - correct answer Lipid transport globule composed of fats mixed with cholesterol and coated with proteins what is a cis fat? - correct answer have both hydrogen atoms on the same side of the double bond; have a kind or bend in the carbon chain, make it difficult for the fatty acids to pack together what is a trans fat? - correct answer hydrogen atoms are on opposite sides of the double bond; trans fatty acids can pack tightly like saturated fats = higher melting point example of cis fat? - correct answer unsaturated natural oils example of trans fat? - correct answer margarine; raises blood cholesterol levels and increases risk of heart disease what makes LDL? - correct answer high cholesterol what is cholesterol needed for? - correct answer synthesize vitamin D in the skin, cholic acid, steroid hormones what don't RBCs have? - correct answer mitochondria what supplies glucose to RBCs? - correct answer cori cycle why does a runner eat high carbs a day before a race? day of? - correct answer day before - gluconeogensis building up for race day; day of - glycolysis because its burned right away

Show more Read less
Institution
Course











Whoops! We can’t load your doc right now. Try again or contact support.

Written for

Course

Document information

Uploaded on
April 6, 2023
Number of pages
33
Written in
2022/2023
Type
Exam (elaborations)
Contains
Questions & answers

Subjects

Content preview

WGU C785 Final Exam Questions and Answers Latest
2022/2023

What is the basic structure of an amino acid? What do they look like? - correct
answer amino group (NH2 or NH3), carboxyl group (COO or COOH), alpha
carbon (C), and variable group

How do you identify the 3 different types of side chains:
non-polar/hydrophobic, polar, and charged? - correct answer
Non-polar/hydrophobic - end with CH or "can't have" water. Polar - end with
OH, SH, or NH. Charged - end with a charge

what kinds of bonds do each of the 3 different types of side chains make? -
correct answer ionic, hydrophobic/non-polar, charged

What are the 4 levels of protein structure? - correct answer Primary - linear
structure, Secondary - Folded into helix or pleated sheet caused by
hydrogen bonding, tertiary - 3D structure caused by side chain interactions,
quaternary - 1+ amino acid chains combine = multiple subunits MUST have
1+ subunit

What enviormental change breaks each type of bond? - correct
answer hydrophobic - temperature change, ionic - salt or decreased
pH, hydrogen - temperature, change in pH, disulfide - reducing agents

what type of amino acid side chain leads to protein aggregration? - correct
answer hydrophobic bonds

how do environmental changes affect protein folding? - correct answer

Extreme temp can cause hydrogen bonds to break apart = malformation of
protein folding

how do mutations affect protein structure? - correct answer Can cause
structure to change. Protein loses form = loses function. May form a different
protein.

What is an electron? - correct answer Negatively charged atom on outer ring
for bonding

,What is energy: - correct answer Power derived fro chemical interaction

what are covalent bonds? - correct answer chemical bond, atoms share 1+
valence electrons

what is an ionic bond? - correct answer bond between positive and negative

what is a hydrogen bond? - correct answer weak bond between positive and
negative

,with an amino? - correct answer piece of amino acid, NH2 or NH3

what is a carboyxl? - correct answer piece of amino acid, COO or COOH

What is hydrophobic? - correct answer Doesn't like water, end with CH

what is hydrophilic? - correct answer Water loving, end with OH, NH, or SH

what is disulfide bond? - correct answer strongest bond between
reduction agents, formed between SH's.

what are zwitterions? - correct answer amino with positive and negative
charges = overall charge of zero

what is a polypeptide - correct answer polymer of amino acids

What is dehydration synthesis? - correct answer Process of forming peptide
bonds

what is hydrolysis? - correct answer adding water to destroy bonds

what is an alpha helix? - correct answer twisted secondary structure,
formed by hydrogen bonds

what is a beta sheet? - correct answer folded second structure shape,
formed by hydrogen bonds

what is denaturation? - correct answer loss of shape duet o interruption of
chemical bonds; occurs via extreme salt, temp, pH

what is aggregation? - correct answer clumping of inner or outer cellular
proteins caused by misfolded proteins leading to diseases such as Alzheimers,
ALS, Parkinson's

how do enzymes catalyze reactions? - correct answer bind with substrates to
decrease activation energy required and decrease reaction rate

how do enzymes affect reaction rate and activation energy? - correct
answer decrease activation energy and decrease reaction rate

, what are the 4 steps of the enzymatic cycle? - correct answer enzyme
recognizes substrate, substrate attracts the enzyme; enzyme-substrate
complex is formed; enzyme-product complex formed; product is released,
enzyme recycled

how do environmental changes affect enzymes? - correct answer High heat,
pH change, high salt concentration, and reducing agents can cause an
enzyme to lose its form/lose function

what is a competitive inhibitor? - correct answer Mimics substrate and
takes its place on the active binding site

Get to know the seller

Seller avatar
Reputation scores are based on the amount of documents a seller has sold for a fee and the reviews they have received for those documents. There are three levels: Bronze, Silver and Gold. The better the reputation, the more your can rely on the quality of the sellers work.
ElonMusk Yale School Of Medicine
Follow You need to be logged in order to follow users or courses
Sold
186
Member since
3 year
Number of followers
163
Documents
1345
Last sold
4 weeks ago
chemistry

FOR THE BEST ASSIGNMENTS AND HOMEWORKS ,TO HELP AND TUTORING ALL KIND OF EXAMS I have done papers of various topics and complexities. I am punctual and always submit work on-deadline. I write engaging and informative content on all subjects. Send me your research papers, case studies, psychology papers, etc, and I’ll do them to the best of my abilities. Writing is my passion when it comes to academic work. I’ve got a good sense of structure and enjoy finding interesting ways to deliver information in any given paper. I love impressing clients with my work, and I am very punctual about deadlines. Send me your assignment and I’ll take it to the next level. I strive for my content to be of the highest quality. Your wishes come first— send me your requirements and I’ll make a piece of work with fresh ideas, consistent structure, and following the academic formatting rules. I'm an expert on major courses especially; All AQA, OCR, A & AS LEVELS AND GCSE, Chemistry, Psychology, Nursing, Mathematics. Human Resource Management. Quality work is my priority. I ensure scholarly standards in my documents. Use my work for GOOD GRADES. In requirement of case studies, test banks, exams and many other studies document our site helps in acquiring them all. If in need of any revision document you can go to the inbox and you will be attended to right away. SUCCESS and BEST OF LUCK.

Read more Read less
4.2

42 reviews

5
27
4
7
3
3
2
1
1
4

Recently viewed by you

Why students choose Stuvia

Created by fellow students, verified by reviews

Quality you can trust: written by students who passed their tests and reviewed by others who've used these notes.

Didn't get what you expected? Choose another document

No worries! You can instantly pick a different document that better fits what you're looking for.

Pay as you like, start learning right away

No subscription, no commitments. Pay the way you're used to via credit card and download your PDF document instantly.

Student with book image

“Bought, downloaded, and aced it. It really can be that simple.”

Alisha Student

Frequently asked questions