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MCAT Biology 1- Biochemistry PART 1

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by: ShayD

MCAT Biology 1- Biochemistry PART 1 CHEM 2223

Marketplace > University of Missouri - St. Louis > Chemistry > CHEM 2223 > MCAT Biology 1 Biochemistry PART 1
GPA 3.74

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About this Document

I recently took a Princeton Review MCAT Boot Camp, and took daily notes on each topic they covered. This specific study guide focuses on the most important information they cover on the MCAT for bi...
Quantitative Analysis
John Gutweiler
Test Prep (MCAT, SAT...)
MCAT, Biology, biochemistry, Enzymes, Enzyme inhibition, Cellular Respiration, Macromolecules, Thermodynamics
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This 9 page Test Prep (MCAT, SAT...) was uploaded by ShayD on Wednesday January 13, 2016. The Test Prep (MCAT, SAT...) belongs to CHEM 2223 at University of Missouri - St. Louis taught by John Gutweiler in Fall 2015. Since its upload, it has received 76 views. For similar materials see Quantitative Analysis in Chemistry at University of Missouri - St. Louis.

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Date Created: 01/13/16
MCAT Biology 1 Review:  *** This study guide will refresh and enhance your knowledge, however it assumes you have a  basic understanding of biology and chemistry***  Amino Acids: α amino group, tetrahedral α carbon, α carboxyl, variable R­ group  Properties: *amphipathic­both hydrophobic/philic (phospholipid bilayer)    Hydrophobic (Non­ Polar): everything else  Hydrophilic: o Polar­ “Threon the Ty rex hates Seared Gluten Crusted Asparagus => Serine,  Cysteine, Tyrosine, threonine, Asparagine, Glutamine o Acid­ has acid in the name o Basic­ “His argument is Lysed” => Lysine, Arginine, Histidine  Structure:  Hydrophobic (Non­ Polar): mostly alkanes R group; rings on proline (cyclobutane ring­  N as R group), phenylalanine, tryptophan; methionine (thioester­ S ether)  Hydrophilic (polar)­ Neutral: Contains an oxygen; tyrosine (thiol ring); cysteine has  sulfhydryl   Hydrophilic (polar)­ Acidic: carboxylic acid as the R group  Hydrophilic (polar)­ Basic: nitrogen containing R groups­ NOT tryptophan  Thermodynamics: does indicate the direction of reaction­ DOESN’T indicate rate  st  1  law conservation of energy  2 law entropy tends to increase; spontaneous reaction tend to increase the disorder   3ed law ∆ G=∆H−T ∆S C ][D ] Q= A [B]  = products/reactants  [ ] ∆G= free energy (energy reactantproducts); Q>1= products, Q<1= reactants  ∆H= enthalpy ∆S= entropy  T=temp. ­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­­ ∆G= ­ negative} spontaneous Exergonic        ∆G= + positive} non spontaneous Endergonic     ∆G= 0} equilibrium  ∆H= ­ negative} exothermic (energy output) ∆H= + positive} endothermic (energy input) Macromolecules:  Proteins: o Basic unit: amino acid  Bonds: covalent peptide bonds (amino acid chains NC) disulfide bridges  (cysteine R groups)   Denature via temperature renders proteins as non­functional  o Structure  Primary­ amino acid sequence peptide bond  Secondary­ initial folding of polypeptide chain: α­ helix or ẞ­ pleated  hydrogen bonds  Tertiary­ folding with hydrophobic amino acid outside disulfide, van der  walls   Quandary­large complexes ­ everything beside covalent (peptide,  disulfide)  Carbohydrates: o Energy storage   Animals­ Glycogen  Plants­ Starch  o Storage=> cellulose (beta­glycosides bonds) cannot digest  o Glyosidic linkages dehydrating reaction   CnH 2n n Don’t forget hydrolysis with macromolecules   Maltose­ glucose+ glucose  Sucrose­ glucose+ fructose  Lactose­ glucose+ galactose  o Formula is to subtract H 2  Lipids: o Roles  Adipose cells­ energy cells  Cellular membrane­ phospholipid barrier, intracellular   Cholesterol­ fluidity and hydrophobic steroid hormones  o  Fatty acid structure: alkanes with carboxylic acid   Saturated (single bond) and unsaturated (double bonds­ “Z or cis”) o Triacylglycerol    Three fatty acid   Glycerol   Bond: ester linkages   R o Phospholipids Lipid bilayer  Phosphate head (hydrophobic)  2x fatty acids   Glycerol  Cholesterol o  general structure:  o Lipoproteins= hormones  Estradiol  Testosterone Enzymes:  Covalent modification: o Adds covalent groups to regulate activity, lifespan, and/or cellular location  Addition if phosphoryl via kinase  Phosphorylation can either activate or inactivate the enzymes    Proteolytic cleavage: o Inactive enzymes (zymogens)­ can be activated via proteases   Association with other polypeptides: can affect enzyme activity  Allosteric regulations­ “on off” mechanism o Regulation not at the active site  Feedback regulation:  o Positive and negative (amplify or diminish final product depending on the amount of product  Enzyme kinetics:  Reaction rate (V) is amount of product formed per unit of time, mol/s o V  maxwhen enzyme is saturated   Adding substrate doesn’t increase rate   Michaelis constant (Km) is the substrate  concentration at which velocity is half its  maximum  After a certain [S] many active sites are  occupied  Inhibition types  Competitive o Compete with substrates for binding sites  Vmax s not affected­ adding most [S] can outcompete inhibitor  It takes more [S] so increasedmK  Noncompetitive o Binds at allosteric site   Vmax s affected but m is no changed since max2  Uncompetitive o Only binds to enzyme­substrate  Cannot bind to[S] o Decreases amount of available enzyme­substrate decrease V  amaxK m  Mixed­type  o May bind either to unoccupied enzyme or enzyme­substrate complex   ∆ Km epends on enzyme affinity to either inhibitor or substrate  Vmax ecreases  Cellular Respiration  Redox Reaction: “oil rig”  oxidation is loss; redox is gain (in chemistry this is elections)  Oxidation  Redox ­Gains oxygen ­ Losses oxygen ­ Losses hydrogen ­ Gains hydrogen ­ Losses electrons ­ Gains electrons  Four stages: o Glucose is split in half – small NADH and ATP glycolysis   Location­ cytosol   Oxygen needed­ NO o Pyruvate is decarboxylated to for acetyl­coA small NADH   Location­ outer mitochondria matrix (entering)  Oxygen needed­ yes; indirectly o acetyl­coA is transformed to form NADH, FADH , small ATP  2  Location­ mitochondria matrix  Oxygen needed yes; indirectly o ETC reduces electron carriers, oxidizes NADH and FADH  ne2ds oxygen  Location­ mitochondria inner membrane   Oxygen needed yes directly  Glycolysis: 2 ATP and 2 NADH with 2 pyruvate  o Old pathway billions of years old Glucose+2ADP+2Pi+2NAD→2 pyruvate+2 ATP+2NADH+2H 2O+2H  Hexokinase­ makes G to G6P (G6P inhibits hexokinase)  Phosphoglucose isomerase­ G F  Phosphofructokinase (inhibited by ATP)­ F­ 1,6­biP  Glyceraldehyde Isomerase­ x2 Gde­3­P  Dehydrogenase­ x2 1,3­biP­Gate  Kinase­ x2 3­P­Gate  Mutase­ x2 2­P­Gate  Enolase­ x2 PEP  Pyruvate Kinase­ x2 Pyruvate  o Phosphofructokinase­ this step we transfer a phosphate group from ATP, PFK is thermodynamically very favorable (practically irreversible); known as the  committed step  Pyruvate Dehydrogenase complex (PDC)­ 2 NADH per glucose  o Pyruvate goes through oxidative decarboxylation, which mean CO  and NAD2 is  produced reducing the pyruvate to a 2 Carbon molecule  This process is done for the two pyruvate molecules   Kreb’s Cycle­ 6 NADH, 2FADH , and 2 2TP per glucose  o Step 1: Acetyl­ coA is combined with oxaloacetate OAA to produce citrate o Step 2: Citrate is oxidized to produce NADH and CO to pro2 ce 4 carbon  Succinate; the 2 original Carbon for acetyl­ coA are conserved    o Step 3: OAA is regenerated, in the process NADH, FADH , and GTP2(all high  energy molecules)  Electron Transport and Oxidative Phosphorylation  o Oxidative Phosphorylation is the oxidation of high energy electron carrier  (NADH and FADH ) 2 o They use 5 electron carriers   3 are large protein carriers found imbedded in the inner mitochondrial  membrane= cytochromes they pump protons out of matrix  2 are small mobile electron carriers  Start from the left to right  1­ NADH dehydrogenase (coenzyme Q reductase)= it “reduces”  NADH’s power  2­ coenzyme Q reductase= ubiquinone get the electrons and passes  them along  3­ cytochrome C reductase  4­ cytochrome C­ small hydrophilic protein  5­ cytochrome C oxidase pump to the final electron accepter  (oxygen)  Energy equivalency o NADH­ 2.5 ATP o FADH ­1.2 ATP o GTP­1 ATP  Energy formations: o Glycolysis 5 ATP (eukaryotes) 7 ATP (prokaryotes) o PDC 5 ATP o Kreb’s Cycle 20 ATP o Total 30 ATP (eukaryotes)/  32 ATP (prokaryotes)  Anaerobic (no oxygen) conditions: o ETC cannot function, and the limited supply of NAD  becomes entirely converted to NADH, so glycolysis still occurs but instead of PDC, pyruvate continues to the  fermentation process  o Fermentation­ two types: (1) reduction of pyruvate to ethanol and (2) the  reduction of pyruvate to lactic acid.  OTHER Metabolic pathways: o Glycogenolysis  Glycogen (polymer of glucose) breakdown, in animal stored as  carbohydrates  Opposite of glycogenesis   Regulated through hormone (glucagon) when blood sugar level are low  o Gluconeogenesis  When no glucose is available  Produces glucose by using lactate, pyruvate and Krebs cycle intermediates  11 step process “glycolysis in reverse” o Pentose phosphate pathway (PPP)    Diverts from G6P in glycolysis, in order to form ribose­5­phosphate to  synthesis nucleotides   Makes NADPH similar to NADH, helps neutralize oxygen species   G6P dehydrogenase primary point of regulations­ vital human  enzyme (deficiency= can lead to death/hepatic complications)  Metabolic regulation­ instead of working at the same time futile cycling, the work in  tight regulation called reciprocal control  o Regulation of glycolysis and gluconeogenesis:  Two regulating enzymes: phosphofructokinase (PFK) and fructose­ 1,6­  biphosphatase (F­1,6­BPase): opposing roles in glycolysis and  gluconeogenesis   Allosterically regulated  o Regulation of the Krebs Cycle  Enzyme: isocitrate dehydrogenase changes based on energy need (high  + NAD , will increase Acetyl­coA)  Pathway Enzyme Positive regulators Negative regulators  Glycolysis Phosphofructokinase fructose­ 2,6­  ATP biphosphatase +  AMP Gluconeogenesis fructose­ 1,6­  fructose­ 1,6­  biphosphatase biphosphatase +  AMP Krebs Cycle isocitrate  ADP ATP+NADH dehydrogenase  Ketogenesis o During period of starvation glycogen stores become exhausted and blood  glucose falls  In response liver makes ketone bodies via Ketogenesis   Can be formed into acetyl­coA  Example is type I diabetes­ ketoacidosis (low blood sugar)  


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