Four Major Organic Compounds. Four organic compounds necessary for life CarbohydratesProteinsLipids Nucleic Acids.

Four Major Organic Four Major Organic CompoundsCompounds

Four organic compounds Four organic compounds necessary for lifenecessary for life

CarbohydratesCarbohydrates

ProteinsProteins

LipidsLipids

Nucleic AcidsNucleic Acids

VocabVocab

Polymer = long molecule consisting of Polymer = long molecule consisting of many similar building blocks linked by many similar building blocks linked by covalent bonds (carbohydrates, proteins, covalent bonds (carbohydrates, proteins, and nucleic acids)and nucleic acids)

Monomer = repeating units that serve as Monomer = repeating units that serve as the building blocks of a polymerthe building blocks of a polymer Example: amino acids are monomers of Example: amino acids are monomers of

proteinsproteins

CarbohydratesCarbohydrates

Preferred energy sourcePreferred energy source Contain Carbon, Hydrogen and Contain Carbon, Hydrogen and

OxygenOxygen Carbo = CarbonCarbo = Carbon Hydrate = Hydrogen and Oxygen in a Hydrate = Hydrogen and Oxygen in a

2:1 ratio (H2:1 ratio (H₂O)₂O)

Simple CarbohydratesSimple Carbohydrates

MonosaccharidesMonosaccharides 3-7 Carbon atoms in backbone3-7 Carbon atoms in backbone Example = GlucoseExample = Glucose

CC₆H₁₂O₆₆H₁₂O₆

1+1= 21+1= 2

Disaccharide = 2 monosaccharides Disaccharide = 2 monosaccharides joined by a covalent bondjoined by a covalent bond

examples: sucrose, lactose, maltoseexamples: sucrose, lactose, maltose

Complex CarbohydratesComplex Carbohydrates

PolysaccharidesPolysaccharides Made of thousands of monosaccharidesMade of thousands of monosaccharides Stored Energy and/or structural Stored Energy and/or structural

componentscomponents Examples= starch, cellulose and Examples= starch, cellulose and

glycogenglycogen

Synthesis of CarbohydratesSynthesis of Carbohydrates

Monomers are joined together and a Monomers are joined together and a molecule of water is lostmolecule of water is lost

Dehydration SynthesisDehydration Synthesis

Decomposition of Decomposition of CarbohydratesCarbohydrates

HydrolysisHydrolysis To break apart using waterTo break apart using water

ProteinsProteins

Functions: messengers, receptors, Functions: messengers, receptors, structural components, muscles, structural components, muscles, enzymesenzymes

Made of amino acids (contain carbon, Made of amino acids (contain carbon, hydrogen, oxygen, nitrogen and hydrogen, oxygen, nitrogen and sometimes sulfur)sometimes sulfur)

Amino Acid structureAmino Acid structure Central carbon group linked to a Central carbon group linked to a

hydrogen, and amino group (NHhydrogen, and amino group (NH₂), an ₂), an acid group (COOH) and a variable group (R)acid group (COOH) and a variable group (R)

Protein FormationProtein Formation Amino acids joined by peptide bonds Amino acids joined by peptide bonds

between the amino group of one and between the amino group of one and the acid group of anotherthe acid group of another

Polypeptide = multiple amino acids Polypeptide = multiple amino acids joined togetherjoined together

Steps to create a functional Steps to create a functional proteinprotein

Primary structure = sequence of Primary structure = sequence of amino acids (polypeptide)amino acids (polypeptide)

Secondary StructureSecondary Structure Chain twists as the result of H+ bonds Chain twists as the result of H+ bonds

between the polypeptide backbonebetween the polypeptide backbone ΑΑ helix = coil from H+ bonds every 4 helix = coil from H+ bonds every 4thth amino acid amino acid ΒΒ sheets = two or more regions of the chain lying sheets = two or more regions of the chain lying

side by side and connected by H+ bondsside by side and connected by H+ bonds

Tertiary Structure = chain folds back Tertiary Structure = chain folds back on itself and creates a globular form on itself and creates a globular form due to interactions between R group due to interactions between R group side chainsside chains Hydrophobic interactions, amino groups Hydrophobic interactions, amino groups

cluster, disulfide bridgescluster, disulfide bridges

Quaternary StructureQuaternary Structure 2 or more tertiary structures combine2 or more tertiary structures combine

How do proteins know how How do proteins know how to properly fold?to properly fold?

Chaperonins = protein molecules Chaperonins = protein molecules that assist in the folding of other that assist in the folding of other proteinsproteins Protect polypeptides from “bad Protect polypeptides from “bad

influences” in the cytoplasm that might influences” in the cytoplasm that might denature the protein or cause it to fold denature the protein or cause it to fold incorrectlyincorrectly

EnzymesEnzymes

Specialized molecules that catalyze Specialized molecules that catalyze reactions in a cellreactions in a cell

Unchanged by the reaction Unchanged by the reaction (reusable)(reusable)

Substrate SpecificSubstrate Specific

Substrate specific (lock and key)Substrate specific (lock and key)

Enzymes ContinuedEnzymes Continued

Can join 2 molecules or separate 1 Can join 2 molecules or separate 1 molecule into 2molecule into 2

Activation energy = energy Activation energy = energy input needed to start a input needed to start a reaction (heat energy)reaction (heat energy)

Enzymes lower activation Enzymes lower activation energy needed for a reactionenergy needed for a reaction

Enzyme + Substrate(s) Enzyme + Substrate(s)

Enzyme Substrate complex Enzyme Substrate complex

Enzyme + Product(s)Enzyme + Product(s)

Active site = substrate specific Active site = substrate specific region on enzymeregion on enzyme

Enzymes are named by their substrate. Enzymes are named by their substrate. The letters The letters asease are added to the are added to the substrates name. Examples are:substrates name. Examples are:

lactase – breaks down lactose (milk sugars)lactase – breaks down lactose (milk sugars)

sucrase – digests complex sugars and starches sucrase – digests complex sugars and starches maltase – digests disaccharides to monosaccharides (malt maltase – digests disaccharides to monosaccharides (malt sugars)  sugars)  glucoamylase – breaks down starch to glucose glucoamylase – breaks down starch to glucose 

protease – breaks down proteins found in meats, nuts, protease – breaks down proteins found in meats, nuts, eggs, and cheeseeggs, and cheese

lipase – breaks down fats found in most dairy products, lipase – breaks down fats found in most dairy products, nuts, oils, and meat nuts, oils, and meat

cellulase – breaks down cellulose, plant fibre; not found in cellulase – breaks down cellulose, plant fibre; not found in humanshumans

Increase temp = increase enzyme Increase temp = increase enzyme activity until optimal temperature activity until optimal temperature reached.reached.

Exceed optimal temp = decrease Exceed optimal temp = decrease enzyme activity (denatures)enzyme activity (denatures)

Enzymes have an optimal pHEnzymes have an optimal pH

Most active at optimal pH less active Most active at optimal pH less active outside of this pH (denature)outside of this pH (denature)

Some molecules can Some molecules can reduce enzyme activityreduce enzyme activity

Competitive inhibitorsCompetitive inhibitors Bind to the active siteBind to the active site Blocking substrates from Blocking substrates from

active siteactive site Noncompetitive inhibitorsNoncompetitive inhibitors

Bind to another part of the Bind to another part of the enzyme (not the active site)enzyme (not the active site)

Cause the enzyme to Cause the enzyme to change shape so substrate change shape so substrate cannot bind to active sitecannot bind to active site

How do enzymes know How do enzymes know when to be active?when to be active?

Allosteric regulationAllosteric regulation Uses regulatory molecules (activators Uses regulatory molecules (activators

and inhibitors) to determine when and inhibitors) to determine when enzymes are activeenzymes are active

ActivatorsActivators Bind to enzyme and stabilize active site Bind to enzyme and stabilize active site

reactions to happenreactions to happen InhibitorsInhibitors

Stabilize the inactive form of the enzyme Stabilize the inactive form of the enzyme prevent reactionsprevent reactions

(Feedback inhibition = the product of the (Feedback inhibition = the product of the enzyme reaction binds to the enzyme and enzyme reaction binds to the enzyme and prevents further reactions)prevents further reactions)