WGU C785 EXAM WITH COMPLETE QUESTIONS AND ANSWERS (VERIFIED ANSWERS) (2026) A!!

WGU C785 EXAM WITH COMPLETE QUESTIONS AND ANSWERS (VERIFIED ANSWERS) (2026) A!! 1. What is the basic structure of an amino acid? What do they look like? - ANSWER amino group (NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C), and variable group 2. How do you identify the 3 different types of side chains: non-polar/hydrophobic, polar, and charged? - ANSWER Non-polar/hydrophobic - end with CH or "can't have" water. Polar - end with OH, SH, or NH. Charged - end with a charge 3. what kinds of bonds do each of the 3 different types of side chains make? - ANSWER ionic, hydrophobic/non-polar, charged 4. What are the 4 levels of protein structure? - 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 5. What environmental change breaks each type of bond? - ANSWER hydrophobic - temperature change, ionic - salt or decreased pH, hydrogen - temperature, change in pH, disulfide - reducing agents 6. what type of amino acid side chain leads to protein aggregation? - ANSWER hydrophobic bonds 7. how do environmental changes affect protein folding? - ANSWER Extreme temp can cause hydrogen bonds to break apart = malformation of protein folding 8. how do mutations affect protein structure? - ANSWER Can cause structure to change. Protein loses form = loses function. May form a different protein. 9. What is an electron? - ANSWER Negatively charged atom on outer ring for bonding 10. What is energy: - ANSWER Power derived fro chemical interaction 11. what are covalent bonds? - ANSWER chemical bond, atoms share 1+ valence electrons 12. what is an ionic bond? - ANSWER bond between positive and negative 13. what is a hydrogen bond? - ANSWER weak bond between positive and negative 14. with an amino? - ANSWER piece of amino acid, NH2 or NH3 15. what is a carboyxl? - ANSWER piece of amino acid, COO or COOH 16. What is hydrophobic? - ANSWER Doesn't like water, end with CH 17. what is hydrophilic? - ANSWER Water Lovering, end with OH, NH, or SH 18. what is disulfide bond? - ANSWER strongest bond between reduction agents, formed between SH's. 19. what are zwitterions? - ANSWER amino with positive and negative charges = overall charge of zero 20. what is a polypeptide - ANSWER polymer of amino acids 21. What is dehydration synthesis? - ANSWER Process of forming peptide bonds 22. what is hydrolysis? - ANSWER adding water to destroy bonds 23. what is an alpha helix? - ANSWER twisted secondary structure, formed by hydrogen bonds 24. what is a beta sheet? - ANSWER folded second structure shape, formed by hydrogen bonds 25. what is denaturation? - ANSWER loss of shape duet o interruption of chemical bonds; occurs via extreme salt, temp, pH 26. what is aggregation? - ANSWER clumping of inner or outer cellular proteins caused by misfolded proteins leading to diseases such as Alzheimers, ALS, Parkinson's 27. how do enzymes catalyze reactions? - ANSWER bind with substrates to decrease activation energy required and decrease reaction rate 28. how do enzymes affect reaction rate and activation energy? - ANSWER decrease activation energy and decrease reaction rate 29. what are the 4 steps of the enzymatic cycle? - ANSWER enzyme recognizes substrate, substrate attracts the enzyme; enzyme-substrate complex is formed; enzyme-product complex formed; product is released, enzyme recycled 30. how do environmental changes affect enzymes? - ANSWER High heat, pH change, high salt concentration, and reducing agents can cause an enzyme to lose its form/lose function 31. what is a competitive inhibitor? - ANSWER Mimics substrate and takes its place on the active binding site 32. what is a noncompetitive inhibitor? - ANSWER Binds to allosteric site causing active site to change shape = preventing substrate from binding with enzyme 33. 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. - ANSWER Inhibitor would cause a build up for product B, decrease product C. Enzyme 3 and product D would not be created. 34. what is substrate? - ANSWER the substance on which an enzyme acts 35. what is a product? - ANSWER result of a reaction 36. what is an intermediate? - ANSWER products produced in an enzyme pathway before final product 37. what is an active site? - ANSWER location where substrate binds with enzyme 38. what is enzyme specificity? - ANSWER Enzymes bind with certain substrate or type of substrate to create a certain reaction 39. what is induced fit? - ANSWER Enzyme changes shape in enzyme-substrate complex to facilitate formation of enzyme-product complex 40. what is kinase? - ANSWER Enzyme, adds phosphate group via phosphorlation 41. what is phosphatase? - ANSWER enzyme, removes phosphate group via dephosphorylation 42. which is an allosteric site? - ANSWER secondary site on an enzyme an inhibitor binds to via non-competitive inhibition 43. what is competitive inhibition? - ANSWER enzyme substrate and inhibitor complex compete to bind with enzyme's active site. no product formed when inhibitor binds with enzyme. 44. what is non-competitive inhibition? - ANSWER inhibitor binds to allosteric site, not active site. Changes shape of active site, preventing substrate from binding and making product 45. what is feedback inhibition? - ANSWER End product sends feedback to beginning of enzyme pathway inhibiting 1st enzyme via noncompetitive inhibition 46. what nucleotides/bases are used in DNA? what are their abbreviations/full names? - ANSWER C - cytosine, G - guanine, A - adenine, T - thyamine 47. what nucleotides/bases are used in RNA? - ANSWER C - cytosine, G - guanine, U - uracil, A - adenine 48. which nucleotides base-pair together in DNA? - ANSWER T-A, G-C 49. which nucleotides base-pair together in RNA? - ANSWER U-A, G-C 50. how to we make complementary DNA? (i.e. coding to temple et reverse) - 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? - 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? - ANSWER Template DNA how do we make protein? - ANSWER DNA - RNA - Protein which type of nucleotide sequence is used and in which direction? - ANSWER RNA is used 5' to 3' what is the relationship between mRNA and tRNA? - ANSWER tRNA is complementary to mRNA how does mRNA splicing allow use to create multiple proteins from a single gene/mRNA? - ANSWER Alternative splicing allows for all introns to be cut and some exons = multiple proteins form from same MRNA what factors increase gene expression? - ANSWER Decreased methylation, increased acetylation, Widely spaced neucleosomes, exposed promoter, use of transcription factors, use RNA polymerase what factors decrease gene expression? - 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? - ANSWER look between the two strands, determine what changed, name the mutation What are the types of mutations? - ANSWER silent, missense, nonsense, frameshift what type of DNA damage does each repair pathway fix? - 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? - ANSWER Recognize damage, cut damage out, recreate DNA strand, glue DNA strand back together what are the steps of mismatch repair? - ANSWER Remove mismatched base, try again what are the steps of homologous recombination and nonhomologous end joining? - 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? - ANSWER denature, anneal, elongation/extension how do we denature DNA in PCR? - ANSWER heat to 95 degrees C to separate DNA strands how do we anneal DNA? - ANSWER primers base pair with DNA strands how do we elongation/extend DNA? - ANSWER DNA polymerase attach primers and synthesize new DNA strands what are the components of PCR? - ANSWER target DNA, heat stable DNA polymerase, nucelotides (dNTP), primers how are primers used to assist in a PCR reaction? - 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? - ANSWER Each cycle produces doubles the amount of DNA how does PCR compare to normal DNA replication in the cell? - 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. Alteration of Protein Structure through Denaturation - ANSWER Protein shape can be altered by breaking the bonds that hold it together Form=function, you break the form you break the function. Denaturation of bonds Disulfide bond: Strong reducing agent Ionic, hydrogen bond: pH change Ionic, hydrogen bond: High salt concentration Hydrophobic interaction: Heat (fever) Misfolding and Aggregation of protiens - ANSWER Ex. Alzhiemers Proteins that denature can aggregate, often this is because of hydrophobic amino acids being exposed. The "clumps" or plaques cannot be broken down and will accumulate to amounts fatal to the cell and cause disease in patients. DNA - ANSWER phosphate + deoxyribose sugar + A/T/C/G Is stored in the nucleus of the cell. Make up of 2 strands mRNA and tRNA they are complimentary pairs that fit together to make the double helix of DNA RNA - ANSWER phosphate + ribose sugar + A/U/C/G nucleic acid - ANSWER is made up of polymers (many monomers) that are called nucleotides. nucleotides - ANSWER Nucleotides contain one or more phosphates, a five-carbon sugar, and a nitrogen base.oNucleotides are always made in the 5' to 3' direction.o5 is always the beginning of the strand, 3 is the end where nucleotides are added. Antiparallel - ANSWER 5' → 3' 3' ← 5' central dogma - ANSWER DNA can not leave the nuclius, so it needs to be copied. Coding DNA → template DNA → mRNA → tRNA (amino acid)DNA →transcribed to mRNA →translated to protein Template DNA - ANSWER DNA is copied into template DNA. That is then transcribed into mRNA (messenger RNA) mRNA - ANSWER Is allowed to leave the nuclius and travel to the main part of the cell called the cytosol. Once in the cytosol it can be picked up by the ribosome Ribosome - ANSWER is the Machine of the cell that makes proteins. Always read mRNA from 5' to 3' reads only 3 bases (codon) at a time it will generate a anticodon that is antiparallel with the mRNA. Translation - ANSWER The ribosome uses the mRNA and tRNA to make a protein. Base Pairing - ANSWER DNA: A → T C → G RNA: A → U C → G C-cytosine G-guanine A-adenine T-thymine DNA only U-uracil. RNA only Sequencing order - ANSWER 1. Coding 2. Template 3. mRNA 4. tRNA what is gene expression? - ANSWER process by which info coded in DNA creates proteins and RNAs What are nucleotides? - ANSWER building blocks of nucleic acids what is antiparallel? - ANSWER refers to arrangement of DNA double helix (run in opposite directions) what is complementary? - ANSWER predictable counterparts what is template DNA? - ANSWER DNA strand, provides pattern for ordering via complementary base pairing in RNA transcript what is coding DNA? - ANSWER nontemplate strand of DNA, same sequence as mRNA except has T instead of U what is replication? - ANSWER processing of copying DNA molecules via DNA synthesis what is transcription? - ANSWER creation of RNA using info from DNA What is RNA polymerase? - ANSWER enzyme, links ribonucleotides to growing RNA chain during transcription what is a promoter? - ANSWER sequence of DNA that binds with RNA, encourages RNA transcription what is a transcription factor? - ANSWER proteins that bind to promoter regions, help initiate transcription what is mRNA? - ANSWER type of RNA, created via DNA template, specifies primary structure of protein what is translation? - ANSWER creation of polypeptide using info in the mRNA what is tRNA? - ANSWER RNA that brings amino acids to ribosomes during creation of polypeptide what are ribosomes? - ANSWER molecular complex, assist with orderly linking of amino acids/polypeptide chains what are codons? - ANSWER nucleotide triplet of DNA or RNA. Basic genetic code. Specifies type of amino acid or termination signal what are anticodons? - ANSWER nucleotide triplet at one end of tRNA. Base pairs with complementary codon on mRNA what is splicing? - ANSWER parts of transcript are removed and others are reconncected what are introns? - ANSWER pieces of noncoding that are removed during RNA processing what are exons? - ANSWER pieces of coding that stay with RNA during processing - ARE NOT DISCARDED what are histones? - ANSWER Protein; high proportion and charged amino acid that binds with DNA. Plays key role in chromatin structure. what is a nucleosome? - ANSWER basic bead like unit of DNA. what is methylation? - ANSWER presence of methyl groups on DNA bases, adding of methyl groups to DNA bases what is acetylation? - ANSWER attachment of acetyl groups to certain amino acids of proteins (mainly histones) what is the structural difference between myoglobin and hemoglobin? - 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? - 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? - 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? - 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? - 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? - ANSWER locks HgB in R-state, and takes up space on HgB for binding to O2 how does it cause carbon monoxide poisoning? - 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? - ANSWER DNA - transcribed - mRNA - translation - protein what is an okazaki fragment? - 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? - ANSWER reduces hemoglobin's affinity for O2 what is the natural function of 2,3-BPG? - ANSWER increases release of O2 in atmosphere with decreased oxygen. efficiently deliver oxygen to fetus. what are we measuring when we measure pH? - ANSWER number of H+ protons in blood what level of pH is blood considered acidic? - ANSWER Below 7.2 what level of pH is blood considered basic? - ANSWER above 7.4 what factors change pH in blood? - ANSWER Increased or decreased CO2, increased or decreased H+ how to do changes in pH affect hemoglobin's structure? - ANSWER Increased CO2/Increased pH = T-state, Decreased CO2/Decreased pH = R-state what is a heme? - ANSWER subunit of hemoglobin/myoglobin what is affinity - ANSWER stickiness of oxygen binding what is cooperativity? - ANSWER binding of O2 to deoxygenated blood what is bicarbonate? - ANSWER carbon dioxide in disguise, outcome of CO2/H2O + carbonic anhydrase what is carbonic anhydrase? - ANSWER enzyme; converts CO2 into bicarb and proton what do chaperones do? - ANSWER assist with protein folding difference between fetal and adult hemoglobin? - 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? - ANSWER Decreased pH = right shift curve. Increased pH = left shift curve. what can show an MI? - ANSWER myoglobin - can show muscle damage Examples of monosaccharides - ANSWER glucose, fructose, galactose examples of disaccharides - ANSWER sucrose, lactose, maltose examples of polysaccharides - ANSWER starch, glycogen, cellulose, chitin how do the different linkages between monomers of polysaccharrides affect how they are digested? - 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? - ANSWER 3 phosphate groups + adenosine. provide energy to cell Polar Covalent Bond - ANSWER An atom bonded to a more electronegative atom. Ionic Bonds - ANSWER Bonds between two atoms so unequal in their attraction for valence electrons that the more electronegative atom strips an electron completely away from its partner. Ion - ANSWER One of two charged atoms resulting from an ionic bond. Cation - ANSWER A positively charged ion Anion - ANSWER A negatively charged ion Ionic compounds - ANSWER Compounds formed by ionic bonds. Stable or Inert Atom - ANSWER An atom with a full valence shell Hydrogen Bonds - ANSWER Relatively weak bonds formed due to the mutual attraction of two electronegative atoms to hydrogen. Compound - ANSWER A substance consisting of two or more elements in a fixed ratio. Element - ANSWER A substance that cannot be broken down into other substances by chemical reactions. Trace Elements - ANSWER Elements required by organisms but only in minute quantities. Two or more atoms held together by a covalent bond consistute a _________. - ANSWER Molecule Octet Rule - ANSWER An atom with more than 1 energy shell is most biologically stable with 8 electrons in the valence shell. Structural Formula - ANSWER Uses bond symbols to show shared electrons between atoms. Example: H-H shows a hydrogen molecule sharing one pair of valence electrons. O=O shows two oxygen atoms sharing two pairs of valence electrons. van der Waals interactions - ANSWER Weak attractions between molecules or parts of molecules that result from transient local partial charges. Reactants - ANSWER The starting materials in a chemical reaction. Products - ANSWER The ending materials in a chemical reaction. O- & NH3+ - ANSWER ionic bond SH +SH - ANSWER disulfide bond reducing agent - ANSWER breaks disulfide bonds OH and NH2 - ANSWER hydrogen bond Ch ch - ANSWER non polar, hydrophobic how can we break charged or Ionic bonds? - ANSWER changes in pH or salt how can we break polar (hydrogen) bonds? - ANSWER changes in pH or salt how can we break nonpolar or hydrophobic bonds? - ANSWER changes in temperature (heat) real-life scenarios that would like to insulin release from pancreas? - ANSWER eating carb rich meal, eating something excessively sugary how does insulin help reduce blood sugar level? - ANSWER promote glycogen formation from excess glucose, stimulates glucose uptake by cells how does glut4 aid in this process? - 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? - ANSWER blood glucose level getting too low due to fasting how can diabetes lead to glycation and AGEs? - 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? - ANSWER breaking down molecules what is anabolism? - ANSWER building up what is a carbohydrate? - ANSWER macromolecule. a type of sugar. What is a monosaccharide? - ANSWER single sugar What is a disaccharide? - ANSWER double sugar What is a polysaccharide? - ANSWER macromolecule; made from hundreds to thounsands of monosaccharides. stores as glycogen and startch. what are alpha linkages? - ANSWER seen in animal polysaccharides. look the same in linkages. what is a beta linkage? - ANSWER seen in plant polysaccharides. face in opposite directions. what is insulin? - ANSWER hormone; lowers blood sugar what is glucagon? - ANSWER hormone; raises blood sugar what is glycogen? - ANSWER form of glucose storage in liver What is glycogenesis? - ANSWER formation of glycogen from glucose what is glut4? - ANSWER glucose transporter what is glycogenolysis? - ANSWER glycogen breakdown, release of glucose what is aerobic metabolism? - ANSWER ATP production using oxygen, breaks down fats and carbs. what is cellular respiratoin? - ANSWER cathbolic pathways of aerobic and anaerboic; break down molecules by using electron trainsport chain for ATP production what is glycolysis? - ANSWER breakdown of glucose, creates 2 new ATP and 2 pyruvate What is the citric acid cycle? - ANSWER creation of 3 NADH and 1 FADH2 and 2 CO2 molecules in each turn of the cycle what is ETC? - ANSWER electron transport chain; accepts electrons from FADH2 and NADH, uses their energy to pump protons to intermember space what does NAD/NADH do? - ANSWER transports electrons of the highest energy to and from complex 1 what does FAD/FADH2 do? - ANSWER transports electrons to/from complex 2 What is substrate level phosphorylation? - ANSWER ATP synthesis by direct transfer of phosphate group to ADP from an intermediate substrate Hydrogen bond - ANSWER Weak bond interaction Between two molecules amino group - ANSWER Consists of hydorgen and nitrogen atoms (-NH3+) macromolecules - ANSWER A giant molecule in a living organism formed by the joining of smaller molecules: a protein, carbohydrate, or nucleic acid. polymer - ANSWER a long molecule consisting of many similar or identical building blocks linked by covalent bonds Amino acid - ANSWER Amino group + Carboxylic acid + R group = Amino acid carboxyl group - ANSWER A -COOH group, found in organic acids. Coo-, O=C-O- Four classes of biological macromolecules - ANSWER Proteins, carbohydrates, nucleic acids, lipids SPONCH - ANSWER Sulfur phosphorous oxygen nitrogen carbon hydrogen polymer - ANSWER a long molecule consisting of many similar or identical monomers linked together by covalent bonds. R group - ANSWER a functional group that defines a particular amino acid that makes it a specific protein (20 amino acids) aka side chain Catalyst - ANSWER Speed up chemical reactions but remain unchanged by the reaction. monomers - ANSWER repeating units that serve as the building blocks of a polymer polysaccharide - ANSWER a polymer of many monosaccharides, formed by dehydration reactions. tertiary structure - ANSWER The third level of protein structure; the overall, three-dimensional shape of a polypeptide due to interactions of the R groups of the amino acids making up the chain. Complex folding- critical to proper functioning Secondary structure - ANSWER Three-dimensional structure of sheets, helices, or other forms taken on by a polypeptide chain, due to electrostatic attraction between neighboring residues. quaternary structure - ANSWER Results from multiple polypeptide subunits. Held together by R group interactions Subunit - ANSWER One of the several polypeptide chains that make up a protein hydrophobic effect - ANSWER Hydrophobic R groups cluster together in the interior of a protein to minimize their contact with water. ( this stabilizes the folded polypeptide backbone) induces aggregation Tertiary structure - ANSWER Three-dimensional structure resulting from folding and covalent cross-linking of a protein hydrogen bond - ANSWER Bonds between hydrogen atom and oxygen atom of another amino acid side chain ( between non-polar amino acids, ends in C-H's) disulfide bond - ANSWER 2 cysteine R groups come together to form a covalent disulfide bond between the 2 sulfur atoms Polar bond - ANSWER a covalent bond in which electrons are shared unequally ( ends in OH or NH or SH or H) polypeptide - ANSWER hundreds of amino acids bonded together in a long chain, sequence of amino acids determines protein hydrophobic - ANSWER a type of weak chemical interaction caused when molecules that do not mix with water coalesce to exclude water. peptide bond - ANSWER the covalent bond between two amino acid units in a polypeptide, formed by a dehydration reaction nucleic acid - ANSWER a polymer (polynucleotide) consisting of many nucleotide monomers; serves as a blueprint for proteins and, through the actions of proteins, for all cellular activities. the two types are DNA and RNA. secondary structure - ANSWER Alpha helix and beta pleated sheet formed through formation of hydrogen bonds., The second level of protein structure; the regular local patterns of coils or folds of a polypeptide chain. tertiary structure - ANSWER the third level of protein structure; the overall, three-dimensional shape of a polypeptide due to interactions of the R groups of the amino acids making up the chain sickle-cell disease - ANSWER A human genetic disease caused by a recessive allele that results in the substitution of a single amino acid in a globin polypeptide that is part of the hemoglobin protein; characterized by deformed red blood cells (due to protein aggregation) that can Atom - ANSWER The basic unit of an element that retains the properties of the element. Proton - ANSWER Positively charged subatomic particle found in the nucleus of an atom; equal to the number of electrons in an electrically neutral atom. Neutron - ANSWER A neutrally charged subatomic particle found in the nucleus of an atom. Electron - ANSWER A negatively charged subatomic particle found orbiting the nucleus of an atom; equal to the number of protons in an electrically neutral atom. Atomic Weight - ANSWER Measured in daltons, and consists of the weight of protons and neutrons together, each of which weighs about one dalton. Orbital - ANSWER The volume of space an electron occupies. Energy Shells - ANSWER Represent the state of potential energy of an electron. Those closer to the nucleus have the least amount of energy. enzymes - ANSWER specialized macromolecules that speed up chemical reactions in cells alpha carbon - ANSWER the central carbon atom of each amino acid Atomic number - ANSWER number of protons atomic mass - ANSWER number of protons plus number of neutrons dehydration synthesis - ANSWER a chemical reaction in which two molecules become covalently bonded to each other with the removal of a water molecule. amino acid backbone - ANSWER The structure comprised of the amino group, carboxyl group with a central alpha carbon atom. dehydration reaction - ANSWER A chemical reaction in which two molecules covalently bond to each other with the removal of a water molecule. Ionic bond - ANSWER formed when two oppositely charged ions attract Hydrophobic - ANSWER non polar, afraid of water Disulfide bond - ANSWER double (di) bond between two Sulfur (sulfide) atoms in cysteine side chains. They stabilize tertiary and quaternary structures of a protein. carbohydrates - ANSWER Organic compounds composed of carbon, hydrogen, and oxygen in a ratio of one carbon atom to two hydrogen atoms to one oxygen atom. They exist as monosaccharides, disaccharides, and polysaccharides. protein - ANSWER a macromolecule consisting of one or more polypeptides chains made up amino acids folded and coiled into a specific three-dimensional structure. polar - ANSWER Amino acid Molecule with partial charges. Mixes with water. covalent bond - ANSWER formed when the difference in electronegativity between A atoms is equal they then share electrons Polar covalent bond - ANSWER when electrons are unequally shared between Atoms because they have different electronegativities Functions of proteins - ANSWER structural support, catalyst, transport, defense, movement, regulation charged - ANSWER Amino acid has a positive or negative charge hydrophobic effect - ANSWER (Water Fearing). Tendency of nonpolar (non charged) substances to aggregate (clump together) in water and exclude the water molecules. amino acid - ANSWER an organic molecule possessing both a carboxyl and an amino group. The monomers of polypeptides. There are 20 different forms. Distinguished by side chains. hydrophobic interactions - ANSWER Interaction between nonpolar molecules in water. Polypeptide - ANSWER A single protein chain formed by amino acids bonded together peptide bond - ANSWER the linkage between amino acids forming a covalent bond between the carboxyl group on one amino acid and the amino group on another, formed by a dehydration reaction. denaturation - ANSWER loss of a proteins normal 3D structure; can possibly be caused by pH and temperature changes which affect the ionic bonds, hydrogen bonds & hydrophilic interactions Hydrolysis - ANSWER Peptide bonds can be broken by this...A chemical process that splits a molecule by adding water. ( this happened frequently in the stomach when proteins begin to bee digested into their amino acids) enzyme - ANSWER a macromolecule serving as a catalyst, a chemical agent that increases the rate of a reaction without being consumed by the reaction. most of them are proteins. Primary Structure - ANSWER Sequence of amino acids forming a protein or polypeptide chain, the most basic element of its structure. What are the functions of carbohydrates - ANSWER function as energy source & structure support; examples: simple sugars, and complex polysacchrides, structural suppport examples: cell wall in pant cells, chitin in insects. cellulose - ANSWER a structural polysaccharide of plant cell walls, consisting of glucose monomers joined by β glycosidic linkages. Quaternary structure - ANSWER Spatial arrangement of two or more individual polypeptide chains. primary structure - ANSWER sequence of amino acids in a polypeptide aka amino acid chain secondary structure - ANSWER Shape formed by hydrogen bonding of amino acid back bone- usually an alpha helix or beta sheet lipids - ANSWER Large, non-polar organic molecules which do not dissolve in water. - fats, phospholipids, steroids, waxes. disaccharide - ANSWER a double sugar, consisting of two monosaccharides joined by a glycosidic linkage formed by a dehydration reaction. What is oxidative phosphorylation? - ANSWER production of ATP using energy derived from ETC reactions; 3rd stage of cellular respiration what is anaerboic metabolism? - ANSWER atp production without oxygen what is fermentation? - ANSWER catabolic process; makes limited amounts of atp without ETC, produces lactic acid or eythl alcohol what is gluconeogensis? - ANSWER formation of glucose from non-carbohydrate sources what is the cori cycle? - ANSWER fermentation + gluconeogenesis, way to make 2 ATP in muscle what is metformin? - ANSWER diabetic medication for Type 2 DM. Decreased gluceoneogensis in liver/increases glucose uptake by muscle what is glycation? - ANSWER colvalent bond of a sugar to a protein What are advanced glycation end products (AGEs)? - 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? - ANSWER transport electrons from CAC to ETC how is NADH generated in glycolysis? - ANSWER glycolysis consumes 2 NAD to create 2 NADH how are NADH and FADH2 generated in the citric acid cycle? - ANSWER each turn of CAC creates 3 NADH molecules and 1 FADH2 how does the ETC use NADH and FADH2? - 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? - ANSWER NADH - complex 1, FADH2 - complex 2 what is the role of the electrons in the ETC? - ANSWER provide energy to pump protons from mitochondrinal space to intermembrane space what is the role of protons in atp product? - ANSWER protons provide energy to make atp as they cross the inner membrane what enyme ultimately makes atp? - ANSWER atp synthase what is the role of oxygen in the ETC? - ANSWER oxygen binds with exhausted electrons from complex 4 to create water how do fats and proteins enter aerobic metabolism? - ANSWER proteins - amino acids - pyruvate or acteyl CoA or CAC. fats - fatty acids - acetyl CoA what are the two different fates of pyruvate? - 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? - ANSWER presence of oxygen in the catabolism how are aerobic and anaerobic metabolism the same? - ANSWER both use glucose, both create ATP and CO2, both use glycolysis in the cytoplasm how are anaerobic and aerobic metabolism the different? - 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? - ANSWER Insulin inhibits: gluconeogensis, glycogenolysis Insulin promotes: Glycolysis, glycogenesis Amino Acid Structure - ANSWER Consist of a Backbone side chain/R group Carboxyl group: Carbon with two attached oxygens Can be COOH or COO- Amino Group: Nitrogen with at least one Hydrogen attached Can be NH2 or NH3+ Alfa Carbon (a carbon): Carbon that sits between amino and carboxyl Hydrogen "hat" Side chain/R group: consists of... Varible group: Unique portion of the amino acid. Amino Acid types - ANSWER Are identified by the R (variable)group. Hydrophobic: no charge, no S, N, or O Polar: no charge, must contain a S,N, or O Charged: Have a Charge Ionic Bonds (Charged amino acids) - ANSWER Two charged amino acids form a iconc bond. Bond disrupted by: pH or Salt concentration Charged amino acids form ionic bonds with other oppositely charged amino acids. Other charges like H+ from pH or salts (charged particles) break up these bonds. Hydrogen Bonds (Polar amino acids) - ANSWER Two polar amino acids form hydrogen bonds Bond disrupted by: pH or Salt concentration Polar forms hydrogen bonds with other polar. Cysteine forms disulfide bonds with other Cysteine. Hydrogen bonds broken by ions like H+ or salt. Disulfide bonds broken by reducing agents Hydrophobic ( non polar amino acids) - ANSWER A bond between two non polar amino acids Nonpolar amino acids form hydrophobic interactions with other nonpolar amino acids only. They do not interact with polar or charged. Located inside of protein to prevent exposure to cytoplasm. Peptide Bond - ANSWER is a chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, releasing a molecule of water (H2O) This is a dehydration synthesis reaction which aerobic and anarobic pathways are controlled by glucagon? - ANSWER Glugcagon promtes: gluconeogensis, glycogenolysis Glucagon inhibits: glycolysis, glycogensis what are the differences between type 1 and types 2 diabetes? - 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? - ANSWER decreases glucogenesis in the liver and increases glucose uptake by the muscle cells how does metformin relate to glut4 and gluconeogensis? - 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? - 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? - 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? - ANSWER from the omega end how do we count carbons in a structure formula? - ANSWER start at end, work your way with smalle groups to write mathematical equation counting carbons in a zig-zag struture? - ANSWER more simplified; carbons at the points (or bends) of zig-zag structure what are the structural differences between saturated and unsaturated fats? - 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? - 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? - 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? - ANSWER cholesterol - membrane buffer/maintain integrity of membrane. phospholipid - major component of cell membrane. triglyceride - ATP storage how do we break down a triglyceride? - ANSWER digested by stomach and small intestine by enzumes such as lipases by using hydrolysis where in the cell does fatty acid breakdown occur? - ANSWER matrix of mitochondria what happens to the different components of the triglyceride? - ANSWER broken into glycerol and fatty acids. picked up by epithelial cells. how do we break down a fatty acid? - ANSWER beta oxidation where in the cell does beta oxidation take place? - ANSWER Fatt acetyl CoA molecules enter mitochondrial matrix and begin beta oxidation cycle what are the 3 products of beta oxidation? - ANSWER 1 acetylCoA, 1 NADH, 1 FADH2 how do we calculate the number of acetylCoA produced from a fatty acid? - 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? - ANSWER one less than the number of acetylCoA moleules produced how do we calculate the amount fo ATP produced? - ANSWER number of acetylCoA molecules mulitplied by 14 what happens to the products of beta oxidation after they are produced? - ANSWER enter ETC for further ATP production how and why are ketone bodies produced? - 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? - ANSWER acetyl-COA how is acetyl-COA exported from the mitochondria to the cytosol? - 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? - ANSWER formation of malonyl COA by acteyl COA carboxylase **needs citrate and CO2** which fatty acid metabolism pathways are controlled by insulin? - ANSWER Insulin encourages lipogensis which fatty acid metabolism pathways are controlled by glucagon? - ANSWER glucagon encourages lipolysis what are the components of the plasma membrane? - ANSWER phospholipids how do cells maintain fluidity of the plasma membrane when moved to colder or warmer temperatures? - ANSWER ratio of saturated/unsaturated fatty acids acting as buffer Amino acid - ANSWER Building blocks of proteins. Amino group + Carboxylic acid + R group = Amino acid Nitrogen with at least one Hydrogen attached Can be NH2 or NH3+ Carbon that sits between amino and carboxyl. Hydrogen "hat" Carbon with two attached oxygens Can be COOH or COO- Primary protein structure: Peptide bonds (backbone) - ANSWER Is a long chain of amino acids formed by peptide bonds. Now forming the backbone of the peptide chain The backbone consists of everything but R groups. This chain is formed by dehydration synthesis - water is removed This chain is broken by hydrolysis - water is added The peptide bond is the defining characteristic of the primary structure. Secondary protein structure: Hydrogen bonds (backbone) - ANSWER Is a long chain of amino acids. With local twists and turns and the backbone is going to interact with it's self via hydrogen bonds Formed by hydrogen bonds between BACKBONE atoms of amino acids. Backbone = everything but R groups. Alpha helix form between amino acids above and below, like a cork screw. Beta sheets can form between amino acids far away. Tertiary protein structure: Hydrophobic interactions, hydrogen bonds, ionic bonds, disulfide bonds (side chain) - ANSWER Is where the different secondaries combined. The protein will move twist and turn to make a 3-D structure where the R groups interact. Hydrophobic interactions play a big role in protein folding. R Group Interactions Hydrophobic interactions - weakest but greatest in number Hydrogen bonds - stronger than hydrophobic Ionic bonds - stronger than hydrogen Disulfide bonds - strongest but fewest in number Quaternary protein structure: More than one subunit held by hydrophobic interactions, hydrogen bonds, ionic bonds, disulfide bonds (side chain) - ANSWER Not all proteins have this. If an amino acid structure can work all by it's self it does not need a Quaternary structure. If the Amino acid has more than one polypeptide chain/subunit held together. Could be as few as two or more than 100 is could be a Quaternary structure. Mutation in protein structure - ANSWER Causes shape change in the beta subunit Leads to aggregation or clumping of the subunits. Ex. sickle cell Mutant hemoglobin will aggregate with other mutant hemoglobin to reduce nonpolar exposure to cytoplasm. Hemoglobin aggregates cannot bind O2 efficiently and also create the cell's sickle shape! what does it mean for a nutrient to be essential? - ANSWER must come from the diet what are the 3 pathways of anerobic metabolism? - ANSWER glycolysis, fermentation, gluconeogensis where in the cell does each pathway take place? - ANSWER Glycolysis - cytoplasm, Fermentation - cytoplasm, Gluconeogensis - liver what are the products of each anaerobic pathway? - 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? - ANSWER fermentation utilized by cells to regenerate NAD what are at least 3 different molecules that can be used as substrates of gluconeogensis? - ANSWER lactate, acteyl COA, glycerol, aminoacids how much atp is used in gluconeogensis? - ANSWER 6 ATP is used what is the net outcome of atp in the cori cycle? - ANSWER Net loss of 4 ATP how does glucagon help increase blood glucose? - ANSWER glucagon promotes release of glucose from energy stores such as liver's glycogen what are the 3 pathways of aerobic metabolism? - ANSWER glycolysis, citric acid cycle, electron transport chain + oxidative phosphorylation where in the cell do the aerobic pathways take place? - ANSWER glycolysis - cytoplasm, citric acid cyle - mitochondrial matix, oxidative phosphorylation/ETC - mitochondrinal inner membrane what molecules are the "ins" of each aerobic pathway? - 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? - 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? - 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? - 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? - 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? - ANSWER glycolysis - 2 ATP, CAC - 2 ATP, ETC - 26 to 28 ATP What are the fat soluble vitamins? - ANSWER A, D, E, K what are the two essential fatty acids and how do we recognize that a fatty acid is essential? - 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? - 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? - ANSWER inflammation, pain, fever, blood pressure, blood clotting, and reproduction how is the function of eicosanoid affected by aspirin? - ANSWER ASA targets eicosanoid production, specifically cox enzymes. decrease prostaglandin production of pain and inflammation what is a saturated fatty acid? - ANSWER fatty acid without double bonds within hydrocarbon chain what is an unsaturated fatty acid? - ANSWER fatty acid with one or more double bonds within hydrocarbon chain What is a triglyceride? - ANSWER a lipid made of one glycerol and three fatty acids what is cholesterol? - ANSWER a steroid; found in animal membranes. has a tetracyclic ring, acts as buffer. what is a phospholipid? - ANSWER similiar to triglycerides; has two fatty acids and one phosphate. love and hates H20 what is a micelle? - ANSWER spherical single layer of phospholipids; transport fatty acids, vitamins, and cholesterol what is an adipocytes? - ANSWER fat cells what is lipase? - ANSWER enzyme that catalyzes triglyceride breakdown what is lipolysis? - ANSWER breakdown of lipids what is beta oxidation? - ANSWER fatty acid breakdown in mitochondria to 1 acetyle COA, 1 NADH, and 1 FADH2 what are ketone bodies? - ANSWER alternative energy form; comes from fatty acid breakdown what is ketoacidosis? - ANSWER accumulation of too many ketones within the body what is MCADD? - ANSWER defect in enzyme used for beta oxidation; need to avoid fasting, eat slow release carbs what is fatty acid synthesis? - ANSWER linking of acetylCOA repeatedly to make new fatty acids in the cytoplasm what is oxaloacetate? - ANSWER Intermediate that couples with acetyl Co-A to form citrate what is citrate? - ANSWER Bridge between carb and fatty acid metabolism; important for fatty acid synthesis what is amphipathic? - ANSWER molecules that are hydrophilic and hydrophobic what is the phospholipid bilayer? - ANSWER polar heads interact with watery environment; nonpolar tails remain inside to avoid water. controls in/out of cell. what is the plasma membrane? - ANSWER boundary of every cell, acts as selective barrier, regulates chemical composition what is a glycolipid? - ANSWER lipid + sugar; bases for A, B, and O blood types what is a glycoprotein? - ANSWER sugar + protein; basis for A, B, and O blood types what is an essential fatty acid? - ANSWER omega 3 and omega 6 fatty acids, must be eat thru diet what is an eicosanoid? - 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? - ANSWER precursor to ecosanoids what is chylomicron? - ANSWER Lipid transport globule composed of fats mixed with cholesterol and coated with proteins what is a cis fat? - 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? - 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? - ANSWER unsaturated natural oils example of trans fat? - ANSWER margarine; raises blood cholesterol levels and increases risk of heart disease what makes LDL? - ANSWER high cholesterol what is cholesterol needed for? - ANSWER synthesize vitamin D in the skin, cholic acid, steroid hormones what don't RBCs have? - ANSWER mitochondria what supplies glucose to RBCs? - ANSWER cori cycle why does a runner eat high carbs a day before a race? day of? - ANSWER day before - gluconeogensis building up for race day; day of - glycolysis because its burned right away Valence Shell - ANSWER The outermost shell of an atom which has the most potential energy. Valence electrons - ANSWER Electrons in the valence, or outermost, energy shell of an atom, which have the most potential energy and which can form bonds with other atoms. Chemical Bonds - ANSWER Attractions between atoms resulting from a sharing of valence electrons or the presence of opposite charges on the atoms. The bonded atoms gain complete valence shells. Covalent Bond - ANSWER The sharing of a pair of valence electrons by two atoms. Molecule - ANSWER Two or more atoms held together by covalent bonds. Single Bond - ANSWER One pair of shared electrons. Example: hydrogen. Double Bond - ANSWER Two pairs of shared electrons. Example: Oxygen has 6 electrons in its valence shell, which can hold 8. Each atom shares 2 electrons for a total of 4. Valence - ANSWER An atom's bonding capacity, or the number of covalent bonds the atom can form to give the atom a full complement of electrons in the valence shell. Usually equals the number of unpaired electrons required to complete the valence shell. Nonpolar Covalent Bond - ANSWER A covalent bond between 2 atoms of the same element in which the electrons are shared equally because the two atoms have the same electronegativity.