Ch 3: Water; Ch 4: Carbon; Ch 5: Large Biomolecules; Ch 8: Metabolism
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tetravalence
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4 bonds->complex molecules
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hydrocarbons
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C and H, release energy
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structural isomer
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differs in covalent arrangement of atoms
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geometric isomer
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differs in spacial arrangements around double bonds
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enantiomer
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mirror image of 4 molecules attached to asymmetric carbon
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-OH
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hydroxyl
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polar/hydrophilic
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-CH3
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methyl
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nonpolar/hydrophobic
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-COOH
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carboxyl
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polar/hydrophilic
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-COH
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carbonyl
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polar/hydrophilic
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-NH2
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amino
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polar/hydrophilic
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-SH
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sulfhydryl
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nonpolar/hydrophobic
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-PO4
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phosphate
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polar/hydrophilic
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Acid
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increases H+ in solution
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Base
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reduces H+ in solution (accepts H+or donates OH-)
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pH
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=-log[H+]
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Buffer
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accepts/donates H+ to stabilize pH
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metabolic pathway
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a specific molecule that is altered in defined steps catalyzed by enzymes that result in a certain product
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catabolic pathway
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releases energy by breaking down complex molecules
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anabolic pathway
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consumes energy to build more complex molecules
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energy
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the capacity to cause change or rearrange matter
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1st Law of Thermodynamics
energy can be transferred and transformed but not created or destroyed
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2nd Law of Thermodynamics
every energy transfer/transformation increases the entropy of the universe; a process must increase entropy to be spontaneous
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Gibbs free energy- ΔG=ΔH-TΔS
energy in a temp/pressure constant system that can perform work
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exergonic
has a net release of free energy (-ΔG)
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endergonic
absorbs free energy (+ΔG)
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ATP
ribose, adenine, 3 phosphate groups
hydrolyzed to ADP+Pᵢ phosphorylated molecules=more reactive |
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Carbohydrates
-monosaccharides held by glycosidic linkages
-energy storage, structure, protection |
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Lipids
-fatty acids held by ester linkages
-hydrophobic, saturated/unsaturated, hormones |
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Nucleic Acids
-nucleotides held by phosphodiester H-bonds
-enable reproduction, controls protein synthesis |
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Proteins
-amino acids held by peptide bonds
-follow varied instructions from DNA |
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Enzymes
these macromolecules act as catalysts that lower activation energy barriers by forming an induced fit w/substrate in the active site
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Enzyme Activation
-gene regulation= enzymes produced when needed
-activators=cofactors (inorganic) and coenzymes (organic) make up and help enzymes function |
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Enzyme Inhibition
-competitive=inhibitor molecule binds to active site to block substrate
-allosteric=inhibitor molecule binds to allosteric site to cover or change shape of the active site |
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Optimal Conditions
-enzymes have optimal temp+pH
-cofactors+coenzymes bind to enzyme or substrate |
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