Biochemistry I

icer215's version from 2016-08-23 02:27

Section 1

Question Answer
FormulaDelta G =Delta H -T Delta S
Delta GGibbs Free Energy
Delta HEnthalpy
T Delta S Temperature/Entropy
Potential energy of rxnDelta H
Kinetic energy of rxnT Delta S
Spontaneous rxnDelta G < 0
EquilibriumDelta G = 0
Non-spontaneousDelta G > 0
Energy of Activationenergy to get transition state and determines rate of rxn

Section 2

Question Answer
Enzymesall are not proteins;must increase rate of rxn;must not get used up in the rxn;specific for a particular rxn;does change the rxn
Substratereactant that interacts with enzyme
Active sitesubstrate binds
Allosteric sitewhere other things bind
Catalystincrease rate of rxn by stabilize T.S. and reducing Ea
Competitive Inhibitionbinds at active site effecton Vmax:unchanged; effecton Km:increases
Non-Competitive Inhibitionbinds at allosteric site:effecton Vmax:decrease;effecton Km:unchanged
Uncompetitive Inhibitionbinds at allosteric site of the ES complex;effecton Vmax:decrease;effecton Km: decrease
Negative Feedbackprovides a shutdown mechanism
Positive Feedbackwhere the product return s to activate the enzyme

Section 3

Question Answer
Four Biologically Macromoleculesproteins, carbohydrates, lipids, & nucleic acids
Dehydration Synthesis condensation; opposite hydrolysis
Proteinsare polymers of amino acids
Amino Acids20 different types
Primary Structurebegin as a straight chain of amino acids;
Disulfide Bridgesometimes chains can bond to each other with two sulfur (S) atoms
Secondary Structurealpha helix and beta pleated sheet; interactions between backbone atoms
Tertiary Structureis the 3D conformation which occurs as a result of the protein folding
Quaternary Structuredetermines the overall shape&binding sites


Question Answer
Prolineplays a central role in the formation of alpha helices and beta sheets. the only cyclic amino acid. It is nonpolar and shares many properties with the aliphatic group. one of the ambivalent amino acids, meaning that it can be inside or outside of a protein molecule.
Aliphatic R groupsare nonpolar and hydrophobic. Gly, Ala, Val, Leu, and Ile. ionization state that predominates at pH 7
Aromaticamino acids are relatively nonpolar. Tyr, Trp, and Phe
Basic amino acidsare polar and positively charged at pH values below their pKa's, and are very hydrophilic. His, Lys, Arg
Hydroxyl amino acidsare polar, uncharged at physiological pH, and hydrophilic. The phenolic hydroxyl ionizes with a pKa of 10 to yield the phenolate anion. Ser, Thr, Tyr
sulfur-containing amino acidsare generally considered to be nonpolar and hydrophobic. Cys and Met
methionineis one of the most hydrophobic amino acids and is almost always found on the interior of proteins.
Cysteineon the other hand does ionize to yield the thiolate anion. can react with other thiol groups in an oxidation reaction that yields a disulfide bond.residues are most frequently buried inside proteins.
LeucineAt physiological pH, exists as a zwitterion. Electrophoretic separation from a protein sample would be least effective at pH 7.4.
isoelectric point for a polypeptideis the pH at which the molecule does not have a net charge.
Electrophoretic separationdepends on the existence of a negative net charge.
Hydrophobic amino acidsprefer to minimize their interactions with water molecules.
Polar, acidic, and basic R groupsall share partial or full charges, which interact favorably with polar water molecules.
All hydrophobic amino acidsshare nonpolar uncharged R groups.

Section 4

Question Answer
Carbohydrates are made up of sugars
Monosaccharide + Monosaccharidedisaccharides
Polysaccharidemultiple monosaccharides
Glycogenanimal glucose
Starchplant glucose storage
Celluloseplant structure
Lipidsmajor function of fats is energy storage
Saturated Fatshave only single carbon-carbon bonds
Unsaturatedcontain one or more carbon-carbon double bonds
Triglyceridesstorage energy
Phospholipidscell membranes
Cholesterolsteroid hormones; e.i. testosterone
Steroidshave a backbone of four interconnected carbon rings
Nucleotidesbuilding blocks of nucleic acids
Ribose 5-carbon sugar
Purineadenine and guanine.
Pyrimidine cytosine and thymine in DNA; cytosine and uracil in RNA
A-T2 hydrogen bonds
C-G3 Hydrogen bonds

Section 5

Question Answer
Oxidation gain oxygen; lose hydrogen; lose e-
Reductionlose oxygen;gain hydrogen; gain e-
Glycolysislocation cytosol;dont need oxygen
Krebs Cycle/PDCmitochondrial matrix; yes, indirect
Electron transport chain/Oxidative Phosphorylationmitochondrial inner; yes, direct
Glycolysisconvert glucose (6 carbons) to 2 molecules of pyruvate (3 carbons);occurs under both aerobic and anaerobic conditions;inhibited by ATP; 2 net ATP made for every glucose (2 input ATP, 4 output ATP);2 NADH made for every glucose.
Krebs cycleacetyl CoA feeds into the cycle;1 ATP (GTP) ,1 FADH2,3 NADH made per acetyl CoA;Inhibited by ATP and NADH
Electron transport chaininput NADH
Anaerobicdon't need oxygen
Aerobicneeds oxygen
Steps of aerobic metabolismglycolysis,oxidative decarboxylation,krebs cycle,electron transport chain
Steps of anaerobic metabolismglycolysis & alcohol or lactic acid fermentation