what are the building blocks of living organisms?
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PO4 2-phosphate (polar)CH3methyl (non polar)the atom carbon is able to form _____ bonds for stability4the atom carbon is able to _____ to other carbonsbindthe atom carbon is able to form complex structures such as _____ and _____rings and chainsthe atom carbon is able to form _____ as well as _____ bondssingle as well as multiple bondsthe atom carbon can demonstrate _____chiralitywhat refers to the ability of a pure isomer to rotate plane polarized light in a lab setting?chiralitychiral carbons have 4 _____ single bonded groupsuniquewhat rotates light clockwise?D (R) isomerswhat rotates light counter clockwise?L (S) isomerswhat contain both isomer forms?racemic mixturesstereochemistry is critically important in what?pharmaceuticalsstereoisomers have the same chemical formula and attachments but differ in their what? this affects binding and affinity; can result in not binding to poorly binding the target affects efficacy.spatial orientationin stereoisomers, incorrect _____ _____ other than the target can be disastrousbinding sitemacromolecules are classified into four main categories, name them.-carbohydrates -lipids -proteins -nucleic acidswhich macromolecules functions in: -energy -storage -structure -cell recognition/communication -modifies proteins affects (structure/folding)(enzyme kinetics)(turnover/degradation)carbohydrateswhat is the structure of carbohydrates?monomer= simple sugarthe ending -ose refers to what?sugarmono, di, and polysaccaride refers to what?the degree of polymerizationD-Glucosealdose (hexose)D-Fructoseketose (hexose)what is an isomer of glucose that has -OH group present on the first carbon atom is on the same side as that of the CH2OH molecule group?alpha glucosewhat is also an isomer of D-glucose in which the -OH group placed on the first carbon atom is placed on the opposite side of the CH2OH group?beta glucosewhat holds together polysaccharides?glycosidic bondstrue or false: alpha bonds are more common than beta bonds?truewhat bonds are easily broken down for energy and modified for storage?alpha 1-4 glycosidic bondssucrose and starch both contain what type of bond?alpha 1-4 glycosidic bondswhat two kinds of bonds does glycogen have? these two bonds gives glycogen its beached structure.-alpha 1-4 bond -alpha 1-6 bondwhat is the primary carbohydrate storage molecule?glycogenwhat type of bond does lactose contain?lactose contains a BETA 1-4 glycosidic bondwhat is the issue with BETA glycosidic bonds?beta bonds are strong, rigid, and are found in cellulose. cellulose cannot be broken down by human digestive enzymes.why might someone who has no problem digesting sucrose or starch have difficulty with lactose?sucrose and starch both contain alpha 1-4 glycosidic bonds which are easy to break down and humans have the digestive enzymes to metabolize these macromolecules lactose has a BETA 1-4 glycosidic linkage which is strong, rigid, and the human digestive enzymes cannot break down this substancealpha glycosidic bonds are hydrolyzed by what?amylasethe BETA bond of lactose requires what in order to be broken down? and why is this an issue?lactose requires LACTASE to be broken down and lactase is only produces in the mucosa of the small intestinelactose intolerance occurs when the body stops producing _____lactaselactose intolerance can form in three ways. what are they?-temporary -genetic -developmentalwhat is an unfortunate circumstance of lactose when it pertains to pharmaceuticals?lactose is a common filler in pharmaceuticalssugar alcohols are formed by the _____ of the carbonyl groupreductionsugar alcohols occur in which pathway?the polyol pathwaywhat is used for storage and can be metabolized forward to fructose or backwards to glucose?sorbitoltrue or false: sorbitol is an EFFECTIVE osmol?truewhat is utilized in signaling, myelin attachment, and nerve function?inositolthe cell _____ the total sugar alcohol levels, such that as one increased the other decreasesregulateshow is glucose transported into cell?glucose is transported into cells by either insulin-dependent or insulin-independent proteinswhat maintains the basal level of glucose required for cell survival?insulin-independent transporter proteinsexcess glucose enter where?the polyol pathwaykidney, retinal, and nerve tissue have a high percentage of what?insulin-independent transportersacidic surges are formed by the _____ of the 6'OH group or the 1'carbonyl group to a carboxyl groupoxidationthe acidic sugar process (oxidation) occurs in many tissues but is highest in what three locations?-liver -kidney -RBCswhat is used as a detoxifying agent? this substance conjugates with molecules to increase solubility and transport or excretion.glucuronic acidwhat is formed by the replacement of an OH group for an NH2 group?amino sugarsglucosamine and galactosamine are amino sugars are compose what?compose the matriculates in connective tissuewhat is between alternating amino sugars that increases the structural nature?beta bondshyaluronic acid and chondroitin are both amino sugars as well as what?connective tissues-modify/regulate protein function -stabilization of proteins in the serum ie antibody Fc fragment -may aid in initial protein folding -aids in cell recognition and binding to membrane proteins -increases hydration of molecule -involved in stabilizing structure these are all characteristics of what?purpose of glycosylationwhat process involves the covalent attachment of many different types of glycans (also called carbohydrates, saccharides, or sugars) to a protein?glycosylationwhat are proteins that are heavily glycosylated? The basic unit consists of a "core protein" with one or more covalently attached glycosaminoglycan chain. The point of attachment is a serine residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge.proteoglycanswhat is a subset of glycoproteins? they are higher in protein content (85% vs 50%) and are primarily found in connective tissue (chondroitin)proteoglycanshow is glycosylation categorized? (hint: this is their bonding/linage)N-linked or O-linkedwhat is it called when the nitrogen atom in the side chain of Asparagine is attached to the sugar?N-linkedwhat linage deals with recognition, binding, and stability (antibodies)?N-linkedwhat is it called when the oxygen atom in the side chain of serine or threonine amino acids is attached to the sugar?O-linkedwhat linkage deals with diverse functions (mucins)?O-linkedwhat macromolecule has functions in: -energy -storage -structure -insulation/protection -hormones -cell signaling?lipidswhat structure has a long chain of hydrocarbons with a terminal carboxyl group?fatty acidswhat is an aromatic structure? this is a deviation of cholesterol.sterolswhat are the two types of fatty acids?saturated and unsaturated fatty acidswhat is a fatty acid that contains all C-C SINGLE bonds?saturatedwhat is a fatty acid that contains one or more C=C double bonds?unsaturatedwhat do double bonds in unsaturated fatty acids cause?kinks within the structurewhich fat is solid at room temperature? this fat comes from mainly red meat animals.saturatedwhich fat is liquid at room temperature? this fat comes from mainly oils in plants.unsaturatedunsaturated fatty acids can be either _____ or _____cis or transwhich type of orientation is more common, cis or trans? this orientation results in a bend.cis_____ fats are less common in nature. the majority of dietary _____ fats are man madetrans, transwhich part of the molecule makes fatty acids acidic?the carboxyl group (OH) at the end of the moleculesteric acid (18:0) -what is the number of carbons? -what is the number of double bonds?-18 carbons -0 double bonds *saturatedoleic acid (18:1 *9) -what does the number 1 indicate? -what does the 9 indicate?-number of double bonds -position of double bondarachidonic acid is an _____ fatty acidessentialunsaturated fatty acids can be classified by _____ _____omega groupsin unsaturated fatty acid nomenclature, how do you base the location of the double bond?from the terminal methyl group (CH3)which type of fatty acids are important in development, neurological functioning, and immune/inflammatory repossess? (ex: linolenic acid and DHA)omega 3what are a diverse group of hormones and signaling molecules produces by the oxidation of fatty acids? particularly arachidonic acid and similar molecules.eicosanoidswhat are the two primary enzymes involved in eicosanoid synthesis?-cyclooxygenases (COX) -lipoxygenases (LOX).what produces prostaglandins and thromboxanes (prostanoids).COXwhat produces produces leukotrienes and lipoxins?LOXthe COX pathway results in molecules with a _____ structurecyclicalprostanoids are locally active hormones/signals which are rapidly _____degradedprostanoids often exhibit _____ functions which are kept in balance during homeostasis and can change/be induced during pathological conditions.opposingfunctions of -inflammation mediation -cardiovascular homeostasis -reproductive function are all characteristics of what?prostanoidsthe LOX pathway produces complex molecules _____ a cyclic component.withoutwhat functions include pro-inflammatory activity and stimulation of immune response?leukotrienewhat functions to resolves inflammation?lipoxinstrue or false: fatty acid monomers do not connect directly to each other?truea connection between fatty acid monomers is made to a 3 carbon sugar alcohol and glycerol through a _____ reactiondehydrationfunctions include: -energy storage -insulation/protection what are these characteristics of?glycerides/acylglycerols_____ start as diacylglycerol with a phosphate group covalently bonded to the third site of the glycerol molecule.phospholipidsthe presence of the phosphate group changes the diacylglcerol to what?phosphatidic acidfunctions include: -membrane structure -signaling -fatty acid reservoir for hormone production what are these characteristics for?phospholipidsphosphatidic acid molecules have a _____ "head" and a _____ "tail" which determines their unique positioning in membrane formation.-hydrophilic head -hydrophobic tailphosphate groups associate with what?aqueous environmentsthe _____ of the fatty acid chains determines the fluidity/reactivity of the membranecompositionincreasing _____ fatty acids increases fluidityunsaturateda saturated lipid membrane would be considered rigid. why?saturated fatty acids have no kinks and therefore they can line up evenlyan unsaturated lipid membrane would be considered fluid. why?unsaturated fatty acids have kinks in them therefore they can cause breaks/spaces within the membranemodification of the phosphate group can alter the _____ of the molecule ex: Phosphatidylcholine component of HDLs increases fluidity yields fatty acids for signaling Phosphatidylinositol high conc. in nerve cells cell attachment/organization signalingfunctionwhat has cholesterol and its derivatives?sterolsfunctions include: -structural component of membranes -hormones -bile salts -vitamins these are characteristics of what?sterols-ol ending indicates the presence of what type of group?alcohol-one or -oid endings are for what?derivativescholesterol embeds in the _____ region of membraneshydrophobiccholesterol _____ the transition state of the membranestabilizesall steroid hormone production beings with cholesterol entering the _____ and undergoing conversion to pregenolonemitochondriawhat can then be converted into mineralcorticoids, glucocorticoids, estrogens, or androgens?pregnenolonewhat is unique about sterile hormone receptor binding?steroids do not bind to the outside of the cell, they pass through the membrane and bind to receptors inside of the celltrue or false: steroid hormones can enter any cell?trueif a steroid hormone receptor is present, the complex becomes a _____ factortranscriptionif there is not a steroid hormone receptor then what happens to the steroid?it can be broken downif there is excess steroid hormone then what happens?excess can be stored in the membranean increased amount of sterols in the membrane increases the membrane's _____rigidityincreased rigidity means there is a decrease in the cells _____reactivitywhat structure produces bile salts to aid in the emulsification of fat in the small intestine?liverbile acids interact with what to form bile salts?Na+what for fat soluble vitamins are based on cholesterol?vitamins A,D,E and Kvitamins A,D,E and K are essential _____ and they need to come from a ore courser or a dietary sourcenutrientsfunctions including: -Structure -Hormones/Signaling -Neurotransmitters -Blood Clotting -Viscosity -Antibodies -Transport -Enzymes these are all characteristics of what?proteinswhat are the monomers for proteins?amino acidschiral isomers in proteins are what form?L formwhat is the point of variation between amino acids?the R groupaspartic acid and glutamic acid are what type of R group?acidiclysine, arginine, and histidine are what type of R group?basicserine, threonine, cysteine, tyrosine, asparagine, and glutamineare what type of R group?polarglycine, alanine, valine, leucine, isoleucine, methioonine, tyrptophan, phenylalanine, and proline are what type of R group?non polarwhat type of reactions form peptide bonds?dehydration reactions-trans configuration -planar -rotation around bond are all bond characteristics of what?peptide bondhow many protein structure levels are there?4what protein structure level is an amino acid sequence that is stabilized by peptide bonds?primarywhat protein structure level has alpha helix, beta pleated sheets and random coils that are stabilized by interactions with primary carbonyl and amine groups? these also form domains.secondarywhat protein structure level has interaction between R groups? interactions include covalent bonding, ionic bonding, hydrophobic interactions, and hydrogen bonding.tertiarywhat protein structure level has interactions between peptide chains? this also has the same bonds as tertiary.quaternarywhat were first identified as heat shock proteins in laboratory experiments?chaperone proteinswhat provide a favorable enlivenment for correct folding, preventing unfolded or partially unfolded proteins from forming aggregates, being degraded, or folding into toxic molecules?chaperone proteinsTriC/CCt is an example of a what? an unfolded enters this structure and then get scolded inside of this structure (into a functioning form)chaperone complexa prion disease results in what?abnormal protein foldingprions are a group of _____ _____ that cause diseases such as bovine spongiform encephalopathy, Creutzfeldt-Jacob, kuru, and fatal familial insomniainfectious proteinsprion proteins occur in what area? prions can also be found to a lesser extent in some tissues.the brainnormal cellular prions appear to have a protective role. which types of prions are protective/helpful?PrP^Cwhat are abnormally folded prions, which form insoluble aggregates called?PrP^SCprotein aggregates _____ neurons and are _____ to degradation-damage -resistantPrP^SC induce PrP^c prions to _____, exponentially increasing the number of dangerous prionsconvertwhat prion disease is found among people from New Guinea who practiced a form of cannibalism in which they ate the brains of dead people as part of a funeral ritual?Kuruwhat disease may occur spontaneously, be inherited, or be transmitted by contact with infected tissue, such as during a transplant or from eating contaminated meat? The condition causes personality changes, anxiety, depression, and memory loss, usually within a few months. Many people lapse into coma.Classic CJD/Mad Cow Diseasewhat is a fatal, degenerative disease affecting the central nervous system of sheep and goats? It is among a number of diseases classified as transmissible spongiform encephalopathies (TSE). Infected flocks can experience significant production losses.scrapieresearch into prion disease has shed light onto disorders such as what two disease? this research does not claim that prions are the source, but it does show the importance of insoluble aggregates/protein buildup within the brain.Alzheimer's and Huntington's Chorearesearch of prions primarily shows the effects of _____ plaque formation and the issue of protein _____-amyloid -misfoldingprion diseases, Alzheimer's and Huntington's Chorea all involve what?neurotoxicityprion misfolding involves the exposure of what?hydrophobic groupsAlzheimer's and Huntington's Chorea both involve problems with post translational modification and hydrophilic _____. neither Alzheimer's or Huntington's Chorea is _____.-interactions -infectionswhat are: -primarily protein based -highly specific for substrate -catalyze all metabolic reactions by lowering the Ea (energy of activation)enzymesreactions are either thermodynamically _____ or _____ based n the charge in free energy.-favorable -unfavorablea negative change results in a _____ reactionspontaneousa positive change will go forward if linked to a strong _____ reactions (such as the hydrolysis of ATP)negativeAn _____ process releases heat, causing the temperature of the immediate surroundings to rise.exothermicAn _____ process absorbs heat and cools the surroundings."endothermicIf the energy level of the reactants is higher than the energy level of the products the reaction is _____ (energy has been released during the reaction).exothermicIf the energy level of the products is higher than the energy level of the reactants it is an _____ reaction.endothermic_____ reactions are spontaneousendothermic_____ reactions are non-spontaneous.exothermicwhat is unlimited? the rate will continue to increase.enzyme concentration [E]what is it when a reaction continues until all the Eisners in the ES complex (Vmax)?substrate concentrationwhat affects charge and reactivity of an active site? the best rate will occur at this optimal.pHwhat rate increase until denaturation occurs?temperatureApoenzyme + prosthetic group =Holoenzyme (functional)what are INORGANIC, usually metal ions (Mg2+, Fe2+, Zn2+), that are required by certain enzymes? Example : ATPases require a Mg2+ to put stress on the high energy bonds.cofactorswhat are ORGANIC molecules such as vitamins and carrier molecules? Example : the complex, pyruvate dehydrogenase, requires thiamine (B1) to act as an electron sink for the carboxylation of pyruvate.coenzymeswhat either prevent the binding of enzymes to a substrate or prevent the enzyme from converting bound substrate to P?inhibitorscompetitive inhibitors resemble what and bind to the active site?resemble the substratewhat bind to an allosteric site and alter the shape of or acmes to the active site?noncompetitive inhibitorswhat can be reversible or irreversible?inhibitionwhat is it called when the enzyme remains functional after removal of the inhibitor?reversible inhibitionwhat is it called when the inhibitor permanently alters the enzyme leaving it nonfunctional?irreversible inhibitionwhat occurs when an enzyme has two binding sites-active and allosteric- for the substrate?substrate level inhibitionthe lower the Km the higher the what?the higher affinity to bindthe higher the Km the the lower what?lower affinity to binda way to regulate too much substrate is to do what?bind to the inhibitory sitebinding at the allosteric site would do what?decrease the binding/conversion at the active sitewhen is substrate level inhibition useful?for metabolic regulation or toxin mitigationwhat catalyzes the first step in the detoxification of alcohol?alcohol dehydrogenasewhat is the most dangerous toxin out of the following choices: -alcohol -acetaldehyde -acetateacetaldehydewhat is a highly toxic molecule that exerts negative effects on the liver and CNS? this also has a complex effect on the cardio vascular system.acetaldehydeby _____ the conversion to the intermediate (acetaldehyde), the most negative effect can be somewhat mitigatedslowingproducts binds to an _____ _____ on the enzyme to slow a reaction downallosteric siteproduct level inhibition is involves in _____ regulationmetabolicExample : Hexokinase and many Krebs Cycle enzymes the product _____ ensures that glucose will not be dedicated to ATP production unless the cell is utilizing it.inhibitionwhat two things tell us the basic information about the enzymes function?Km and VmaxKm refers to the _____ of the E for the S; the LOWER the Km the HIGHER the affinityaffinityVmax gives you insight into the _____ of the E to handle fluctuations; Vmax is when ALL E is in the ES complexcapacitywhat catalyze the same reaction but due to minor structural changes, have different activity levels?isoenzymeswhat are found in most tissues and is considered the maintenance enzyme?hexokinaseswhat enzyme is found primarily in the liver? this is technically a very specific form of hexokinase.glucokinaseG-6-P can be directed to _____ _____ synthesis, as well as, to _____ _____-glycogen synthesis -cellular respirationunder conditions of high _____ and low _____ certain Kreb's Cycle enzymes are not going to move the process forward-high ATP -low ADPbuildup of _____ will stimulate the biosynthesis of fatty acidscitrateExplain what would happen to the liver in a consistently high sugar environment?The liver is able to create a lot of G-6-P and has no product inhibition....the liver can be upregulated and can make glycogen or fatwhat are tissue specific? their presence in the blood is indicative of damage to a specific tissue type.isoenzymeswhat biomarker of isoenzymes signals that a cell is damaged: CPK1brain and lungswhat biomarker of isoenzymes signals that a cell is damaged: CPK2heartwhat biomarker of isoenzymes signals that a cell is damaged: CPK3skeletal muscleswhat functions include: -genetic information -direct protein synthesis -energy -neurotransmittersnucleic acidsnucleic acids such as _____ and _____ are made up of nucleotide monomersDNA and RNAwhat is an example of a DNA monomer?AMPnitrogenous base, ribose sugar, phosphate base are all components of what?components of nucleotidewhat is the sugar in RNA?ribosewhat is the sugar in DNA?deoxyribosecytosine (C) uracil (U) *only in RNA thymine (T) *in DNA are all components of what?pyrimidinesguanine (G) adenine (A) are all components of what?purinesnucleotides bind so that the 3-OH group of one attaches to the 5' _____ of the otherphosphatein a chain, the polymer will only attach new monomers to which end?3'what is the most common DNA structure? this isa RIGHT handed helix. this is also the normal shape that gets used as a template.B DNAwhich DNA is shorter, more dense, right handed helix, RNA-DNA complex, double stranded RNA regions? this is only a temporal DNA used during transcription.A DNAwhich DNA is longer, stretches out, left handed helix, increased methylation, shut down? this DNA type CANNOT be transcribed.Z DNAwhat is the coded message that directs peptide synthesis?mRNAwhat stabilizes mRNA in the ribosome?rRNAwhat transfers amino acids to ribosome for peptide construction?tRNAwhat is heterogenous nuclear RNA that is the unedited mRNA? this contains introns that must be removed. *only found in eukaryotic cells and never leaves the nucleus* includes axons (expressed) and introns (interfere and must be removed). this is the RAW MESSAGE.hnRNAwhat is small nuclear RNA? this forms complexes with proteins forming snRNPs. this performs splicing of hnRNAs to produce mRNAs. *never leaves the cell.snRNAwhat is an enzyme that synthesizes short RNA sequences called primers?primaseWithin each fork, one DNA strand, called the _____ strand, is replicated continuously in the same direction as the moving fork, while the other _____ strand is replicated in the opposite direction in the form of short _____ _____-leading -lagging -Okazaki fragments.DNA _____ is a specific type of enzyme, that facilitates the joining of DNA strands together by catalyzing the formation of a phosphodiester bond. It plays a role in repairing single-strand breaks in duplex DNA in living organisms, but some forms may specifically repair double-strand breaks.ligasewhat is the point at which the two strands of DNA are separated to allow replication of each strand.replication forkwhat contain high energy bonds ex: ATPenergy moleculeswhat holds a high amount of energy that is released due to stress/tension?high energy bondadenosine is simply the nucleotide without the phosphate group. this is also known as a what?neurotransmitter